分类： 生长因子growth factors

ProSpec-Activin A Human/CYT-569

ProSpec-Activin A Human,如果整个小瓶将在 2-4 周内使用，请在 4°C 下储存。 储存，在 -20°C 下冷冻更长时间。
对于长期储存，建议添加载体蛋白。
避免多次冻融循环。

  • Activin A Human

  • Activin A Human Recombinant
  • CYT-569

Catalogue number

CYT-569

Synonyms

Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.

Introduction

Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.
抑制素是由雌性卵巢颗粒细胞和雄性支持细胞以及多种其他组织产生的二聚肽激素。 抑制素有两种同工型，A 和 B，具有相同的 α 亚基但不同的 β 亚基。 抑制素A是α和βA亚基的二聚体，抑制素B是α和βB亚基的二聚体。
抑制素被认为可以抑制垂体产生促卵泡激素。 此外，抑制素还被认为在控制配子发生、胚胎和胎儿发育中发挥作用。

Description

Activin-A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 137 amino acids and having a molecular mass of 15.2kDa.
Activin-A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
在大肠杆菌中产生的 Activin-A Human Recombinant 是一条单一的、非糖基化的多肽链，包含 137 个氨基酸，分子量为 15.2kDa。
Activin-A 在 N 末端与 20 个氨基酸的 His-tag 融合，并通过专有色谱技术进行纯化。

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

Activin-A protein solution contains 20mM Tris pH 8.0 and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.
如果整个小瓶将在 2-4 周内使用，请在 4°C 下储存。 储存，在 -20°C 下冷冻更长时间。
对于长期储存，建议添加载体蛋白。
避免多次冻融循环。

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Related Products

  • Activin-A Human Active
  • Activin B Human
  • Activin-A Human Plant-Active
  • Activin-A Mouse
  • Inhibin alpha A Chain Human
  • Activin B Human Active
  • Activin-A Rat
  • Activin A Human Plant
  • Activin-A Antibody
  • Inhibin a Human

ProSpec-Activin A Human Plant,CYT-052

Activin A human Recombinant 生产于本氏烟草植物中，是二硫键连接的两条 betaA 链的同源二聚体，每条链含有 116 个氨基残基和 N 端的 6-His-tag，总分子量为 27.4kDa。

  • Activin A Human Plant
  • Activin A Human Recombinant, Plant
  • CYT-052

Catalogue number

CYT-052

Synonyms

Inhba, Inhibin beta A, FSH releasing protein.

Introduction

Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits . Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
激活素是同源二聚体还是异源二聚体？ 亚基异构体，TGF 的一部分？ 家庭。 成熟的激活素 A 有两个 116 个氨基酸残基的 betaA 亚基。 Activin 具有广泛的生物活性，包括中胚层诱导、神经细胞分化、骨重塑、造血和生殖生理学。 激活素参与 FSH、LH、GnRH 和 ACTH 等激素的产生和调节。 经鉴定表达激活素 A 的细胞包括成纤维细胞、内皮细胞、肝细胞、血管平滑肌细胞、巨噬细胞、角质形成细胞、破骨细胞、骨髓单核细胞、前列腺上皮细胞、神经元、软骨细胞、成骨细胞、间质细胞、支持细胞和卵巢颗粒细胞 .

Description

Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.
Activin A human Recombinant 生产于本氏烟草植物中，是二硫键连接的两条 betaA 链的同源二聚体，每条链含有 116 个氨基残基和 N 端的 6-His-tag，总分子量为 27.4kDa。

Source

Nicotiana benthamiana plant

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from 1mg/ml solution in Tris HCl 0.05M buffer at pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized Activin A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Activin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin A should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 97.0% as determined by Analysis by -PAGE.

Amino acid sequence

HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

Serological Identification

The protein was electrophoresed under reducing condition on a 15% -polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin A.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Related Products

  • Activin-A Rat
  • Activin A Human
  • Activin B Human
  • Activin-A Antibody
  • Activin-A Human Active
  • Activin B Human Active
  • Activin-A Human Plant-Active
  • Activin-A Mouse

ProSpec-Activin B Human

ProSpec-Activin B Human,本氏烟草植物中产生的 Activin B human Recombinant 是一种含有 123 个氨基酸的 β-B 单链。 激活素 B 在 N 端与总分子量为 14kDa 的 10-His 标签融合，并通过标准色谱技术进行纯化。

 

  • Activin B Human

  • Activin-B Human Recombinant
  • CYT-058

Catalogue number

CYT-058

Synonyms

Inhibin beta B , Inhibin, beta-2, Activin beta-B chain, MGC157939.

Introduction

Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.
抑制素是由雌性卵巢颗粒细胞和雄性支持细胞以及多种其他组织产生的二聚肽激素。 抑制素有两种同工型，A 和 B，具有相同的 α 亚基但不同的 β 亚基。 抑制素A是α和βA亚基的二聚体，抑制素B是α和βB亚基的二聚体。
抑制素被认为可以抑制垂体产生促卵泡激素。 此外，抑制素还被认为在控制配子发生、胚胎和胎儿发育中发挥作用。

Description

Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain containing 123 amino acids . Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.
本氏烟草植物中产生的 Activin B human Recombinant 是一种含有 123 个氨基酸的 β-B 单链。 激活素 B 在 N 端与总分子量为 14kDa 的 10-His 标签融合，并通过标准色谱技术进行纯化。

Source

Nicotiana benthamiana plant

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.
冻干的 Activin B 虽然在室温下可稳定保存 3 周，但应在 -18°C 以下干燥储存。 复溶后，Activin B 应在 4°C 下储存 2-7 天，以备将来在 -18°C 以下使用。 对于长期储存，建议添加载体蛋白。
请防止冻融循环。

Purity

Greater than 97.0% as determined by Analysis by -PAGE.

Amino acid sequence

HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Related Products

  • Activin B Human Active
  • Activin-A Human Plant-Active
  • Activin A Human
  • Activin A Human Plant
  • Activin-A Antibody

ProSpec-Activin B Human Active

  • Description

  • Activin B Human Active

  • Activin-B Human Recombinant, Active
  • CYT-057

Catalogue number

CYT-057

Synonyms

Inhibin beta B , Inhibin, beta-2, Activin beta-B chain, MGC157939.

Introduction

Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

Description

Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain containing 123 amino acids . Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

Source

Nicotiana benthamiana plant

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 97.0% as determined by Analysis by -PAGE.

Amino acid sequence

HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG.

Biological Activity

The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Related Products

  • Activin-A Human Plant-Active
  • Activin A Human
  • Activin-A Antibody
  • Activin A Human Plant
  • Activin B Human

ProSpec-Activin-A Human Active

  • Description

  • Activin-A Human Active

  • Activin-A Human Recombinant, Active
  • CYT-145

Catalogue number

CYT-145

Synonyms

Inhba, Inhibin beta A, FSH releasing protein.

Introduction

Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits . Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

Description

Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.
The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Physical Appearance

Lyophilized freeze dried powder.

Formulation

Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

Solubility

Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95% as obsereved by -PAGE.

Amino acid sequence

MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

Biological Activity

Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Related Products

  • Activin-A Rat
  • Activin A Human Plant
  • Activin A Human
  • Activin-A Human Plant-Active
  • Activin-A Mouse

ProSpec-Activin-A Human Plant-Active

  • Description

  • Activin-A Human Plant-Active

  • Activin-A Human Recombinant, Plant-Active
  • CYT-414

Catalogue number

CYT-414

Synonyms

Inhba, Inhibin beta A, FSH releasing protein.

Introduction

Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits . Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

Description

Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.
The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.

Source

Nicotiana benthamiana.

Physical Appearance

Lyophilized freeze dried powder.

Formulation

Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4

Stability

For long term storage it is recommended to add a carrier protein . Repeated freezing and thawing is not recommended.

Solubility

INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.

Amino acid sequence

HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

Biological Activity

The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line cells proliferation . ED50<5ng/ml.

Purity

Greater than 98% as obsereved by -PAGE.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Related Products

  • Activin-A Antibody
  • Activin A Human
  • Activin A Human Plant
  • Activin-A Human Active
  • Activin B Human
  • Activin-A Mouse
  • Activin B Human Active
  • Activin-A Rat

ProSpec-Activin-A Mouse

  • Description

  • Activin-A Mouse

  • Activin-A Mouse Recombinant
  • CYT-146

Catalogue number

CYT-146

Synonyms

Inhba, Inhibin beta A, FSH releasing protein.

Introduction

Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits . Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

Description

Active form Activin-A Murine Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.
The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Physical Appearance

Lyophilized freeze dried powder.

Formulation

Mouse Activin-A lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

Solubility

Murine INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95% as obsereved by -PAGE.

Amino acid sequence

MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

Biological Activity

Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Related Products

  • Activin-A Human Active
  • Activin-A Human Plant-Active
  • Activin A Human Plant
  • Activin A Human
  • Activin-A Rat

ProSpec-Activin-A Rat

  • Description

  • Activin-A Rat

  • Activin-A Rat Recombinant
  • CYT-147

Catalogue number

CYT-147

Synonyms

Inhba, Inhibin beta A, FSH releasing protein.

Introduction

Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits . Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

Description

Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.
The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Physical Appearance

Lyophilized freeze dried powder.

Formulation

Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.

Solubility

Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95% as obsereved by -PAGE.

Amino acid sequence

MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

Biological Activity

Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 1-1.5 ng/ml corresponding to a specific activity of 666,667-1,000,000 Units/mg.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Related Products

  • Activin A Human
  • Activin A Human Plant
  • Activin-A Human Active
  • Activin-A Mouse
  • Activin-A Human Plant-Active

ProSpec-ACVR1 Human

  • Description

  • ACVR1 Human

  • Activin A Receptor Type 1 Human Recombinant
  • CYT-1140

Catalogue number

CYT-1140

Synonyms

ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.

Introduction

Activin A Receptor Type 1 is a member of TGF-beta serine/threonine kinase receptor family. ACVR1 forms a receptor complex contains2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate,bind and activate SMAD transcriptional regulators. ACVR1 takes part in left-right pattern formation during embryogenesis and is also essential in the BMP pathway which is responsible for the development and repair of the skeletal system.ACVR1 is linked to Fibrodysplasia Ossificans Progressiva which isknown for the formation of heterotopic bone throughout the body.

Description

ACVR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids and having a molecular mass of 38.4kDa.
ACVR1 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

ACVR1 protein solution contains Phosphate Buffered Saline and 10% glycerol. 

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-ACVR2A Human

  • Description

  • ACVR2A Human

  • Actv Receptor Type 2A Human Recombinant
  • CYT-976

Catalogue number

CYT-976

Synonyms

ACVR2A, ACTRIIA, ACTR-IIA,

Introduction

ACVR2A takes part in various biological processes including mesoderm induction, neural cell differentiation, bone remodeling, hematopoiesis, carcinogenesis, and inflammation. ACVR2A which is a receptor for Actv A, Actv B and inhibin A mediates induction of adipogenesis by GDF6.

Description

ACVR2A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 124 amino acids and having a molecular mass of 14.4kDa .
ACVR2A is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

ACVR2A protein solution containing Phosphate Buffered Saline and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 95% as determined by -PAGE.

Amino acid sequence

AILGRSETQE CLFFNANWEK DRTNQTGVEP CYGDKDKRRH CFATWKNISG SIEIVKQGCW LDDINCYDRT DCVEKKDSPE VYFCCCEGNM CNEKFSYFPE MEVTQPTSNP VTPKPPLEHH HHHH.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-ACVRL1 Human

  • Description

  • ACVRL1 Human

  • Activin A Receptor Type II-Like 1 Human Recombinant
  • CYT-920

Catalogue number

CYT-920

Synonyms

Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.

Introduction

Activin A Receptor Type II-Like 1, also known as ACVRL1 is a membrane-anchored proteoglycan which his core protein binds TGFf3 and has a short cytoplasmic domain with no discernible signaling structure. Furthermore, ACVRL1 shares similar domain structures with other closely related ALK or activin receptor-like kinase proteins which form a subfamily of receptor serine/threonine kinases.

Description

ACVRL1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 103 amino acids and having a molecular mass of 11.5kDa. .
ACVRL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

ACVRL1 protein solution contains phosphate buffered saline and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSE

QPGTDGQHHH HHH.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-CSF2RA Human

  • Description

  • CSF2RA Human

  • GM-CSF Receptor Alpha Human Recombinant
  • CYT-796

Catalogue number

CYT-796

Synonyms

CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.

Introduction

GM-CSF Receptor Alpha is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.

Description

CSF2RA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids and having a molecular mass of 37.2kDa.

CSF2RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

CSF2RA protein solution containing 20mM Tris-HCl buffer , 0.4M urea and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 85.0% as determined by -PAGE.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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  • CSF2RA Human, sf9

ProSpec-CSF2RA Human, sf9

  • Description

  • CSF2RA Human, sf9

  • GM-CSF Receptor Alpha Sf9 Human Recombinant
  • CYT-1044

Catalogue number

CYT-1044

Synonyms

Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity , Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX,  GMCSFR, CD116, SMDP4, GMR.                  

Introduction

GM-CSF Receptor Alpha is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.

Description

CSF2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids and having a molecular mass of 35.9kDa. . CSF2RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

CSF2RA protein solution contains Phosphate Buffered Saline and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. 

For long term storage it is recommended to add a carrier protein . 

Avoid multiple freeze-thaw cycles.

Purity

Greater than 90.0% as determined by -PAGE.

Biological Activity

Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

Amino acid sequence

ADPLIPEKSD LRTVAPASSL NVRFDSRTMN LSWDCQENTT FSKCFLTDKK NRVVEPRLSN NECSCTFREI CLHEGVTFEV HVNTSQRGFQ QKLLYPNSGR EGTAAQNFSC FIYNADLMNC TWARGPTAPR DVQYFLYIRN SKRRREIRCP YYIQDSGTHV GCHLDNLSGL TSRNYFLVNG TSREIGIQFF DSLLDTKKIE RFNPPSNVTV RCNTTHCLVR WKQPRTYQKL SYLDFQYQLD VHRKNTQPGT ENLLINVSGD LENRYNFPSS EPRAKHSVKI RAADVRILNW SSWSEAIEFG SDDGHHHHHH

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-CSF2RB Human

  • Description

  • CSF2RB Human

  • GM-CSF Receptor Beta Human Recombinant
  • CYT-928

Catalogue number

CYT-928

Synonyms

CSF2RB,Colony Stimulating Factor 2 Receptor, Beta, Low-Affinity , GM-CSF/IL-3/IL-5 Receptor Common Beta Subunit, CDw131, IL3RB, SMDP5, IL5RB, Interleukin 3 Receptor/Granulocyte-Macrophage Colony Stimulating Factor 3 Receptor, Beta , Colony-Stimulating Factor-2 Receptor, Beta, Low-Affinity, GM-CSF/IL-3/IL-5 Receptor Common Beta-Chain, Cytokine Receptor Common Subunit Beta, CD131 Antigen, CD131.

Introduction

GM-CSF Receptor Beta, also known as CSF2RB is a member of the type I cytokine receptor family. CSF2RB is a high affinity receptor for interleukin-3, interleukin-5 as well as granulocyte-macrophage colony-stimulating factor. CSF2RB unique form of receptor assembly applies also to IL-3 and IL-5 receptors, providing a structural basis for understanding their activation mechanism which is essential for the development of therapeutics.

Description

CSF2RB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 435 amino acids and having a molecular mass of 49.7kDa.
CSF2RB is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered clear solution.

Formulation

CSF2RB protein solution containing Phosphate Buffered Saline and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

WERSLAGAEE TIPLQTLRCY NDYTSHITCR WADTQDAQRL VNVTLIRRVN EDLLEPVSCD LSDDMPWSAC PHPRCVPRRC VIPCQSFVVT DVDYFSFQPD RPLGTRLTVT LTQHVQPPEP RDLQISTDQD HFLLTWSVAL GSPQSHWLSP GDLEFEVVYK RLQDSWEDAA ILLSNTSQAT LGPEHLMPSS TYVARVRTRL APGSRLSGRP SKWSPEVCWD SQPGDEAQPQ NLECFFDGAA VLSCSWEVRK EVASSVSFGL FYKPSPDAGE EECSPVLREG LGSLHTRHHC QIPVPDPATH GQYIVSVQPR RAEKHIKSSV NIQMAPPSLN VTKDGDSYSL RWETMKMRYE HIDHTFEIQY RKDTATWKDS KTETLQNAHS MALPALEPST RYWARVRVRT SRTGYNGIWS EWSEARSWDT ESVLPMWLEH HHHHH.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-G CSF Human

  • Description

  • G CSF Human

  • Granulocyte-Colony Stimulating Factor Human Recombinant
  • CYT-220

Catalogue number

CYT-220

Synonyms

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.

Introduction

GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8 KD.
GCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

GCSF was lyophilized after extensive dialysis against 10mM sodium acetate buffer pH= 4.

Solubility

It is recommended to reconstitute the lyophilized GCSF in sterile 20mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Amino acid sequence

The sequence of the first five N-terminal amino acids of GCSF was determined and was found to be Met-Thr-Pro-Leu-Gly.

Purity

Greater than 98.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.

Protein content

GCSF quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.815 as the extinction coefficient for a 0.1% solution. This value is calculated by the PC GENE computer analysis program of protein sequences .
2. Analysis by RP-HPLC, using a calibrated solution of GCSF as a Reference Standard.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

References

Title:Contribution of an Aged Microenvironment to Aging-Associated Myeloproliferative Disease.
Publication:Vas V, Wandhoff C, Dörr K, Niebel A, Geiger H Contribution of an Aged Microenvironment to Aging-Associated Myeloproliferative Disease. PLoS ONE 7: e31523. doi:10.1371/journal.pone.0031523
Link:http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0031523

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ProSpec-G CSF Human, CHO

  • Description

  • G CSF Human, CHO

  • Granulocyte-Colony Stimulating Factor Human Recombinant, CHO
  • CYT-329

Catalogue number

CYT-329

Synonyms

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Introduction

Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.

Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in CHO cells is a single, glycosylated, polypeptide chain containing 174 amino acids and having a molecular mass of approximately 18 kDa.
G-CSF is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells .

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

G-CSF was lyophilized from a concentrated solution containing 10mM Hydrochloric Acid pH=6.5, 0.4mg tween 20, 100mg mannitol, 160mg L-arginine, 40mg phenylalanine and 4mg methionine.

Solubility

It is recommended to reconstitute the lyophilized Granulocyte Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Granulocyte Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution G-CSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Amino acid sequence

TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL GHSLGIPWAP LSSCPSQALQ LAGCLSQLHS GLFLYQGLLQ ALEGISPELG PTLDTLQLDV ADFATTIWQQ MEELGMAPAL QPTQGAMPAF ASAFQRRAGG VLVASHLQSF LEVSYRVLRH LAQP.

Purity

Greater than 97.0% as determined by -PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells is < 0.07 ng/ml, corresponding to a Specific Activity of 1.27 x 108 IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-G CSF Human, HEK

  • Description

  • G CSF Human, HEK

  • Granulocyte-Colony Stimulating Factor Human Recombinant, HEK
  • CYT-088

Catalogue number

CYT-088

Synonyms

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Introduction

GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

Description

G-CSF Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 21-25kDa due to glycosylation.
The G-CSF is purified by proprietary chromatographic techniques.

Source

HEK.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The G-CSF was lyophilized from 1mg/ml in 1xPBS.

Solubility

It is recommended to reconstitute the lyophilized G-CSF in sterile 1xPBS containing 0.1% endotoxin-free recombinant HSA.

Stability

Lyophilized G-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution G-CSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95% as obsereved by -PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells , the ED50 is <0.01ng/ml.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-G CSF Human, His

  • Description

  • G CSF Human, His

  • Granulocyte-Colony Stimulating Factor Human Recombinant, His Tag
  • CYT-476

Catalogue number

CYT-476

Synonyms

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Introduction

Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.

Description

Granulocyte Colony Stimulating Factor-His Tag Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids, fragment and having a molecular mass of 23.19 kDa with an amino-terminal hexahistidine tag.
G-CSF-His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

Granulocyte Colony Stimulating Factor His is supplied in 1x PBS and 50% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
Please avoid freeze thaw cycles.

Purity

Greater than 95.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-G CSF Human, PEG

  • Description

  • G CSF Human, PEG

  • Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant
  • CYT-018

Catalogue number

CYT-018

Synonyms

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Introduction

GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa.
G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Colorless, clear and transparent solution.

Formulation

G-CSF is supplied in solution containing 10mM Acetate Buffer , and 0.004% Polysorbate 80.

Stability

G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use.
Shaking and freezing should be avoided.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-G CSF Mouse

  • Description

  • G CSF Mouse

  • Granulocyte-Colony Stimulating Factor Mouse Recombinant
  • CYT-410

Catalogue number

CYT-410

Synonyms

CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.

Introduction

Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.

Description

Granulocyte Colony Stimulating Factor Mouse Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 178 amino acids and having a molecular mass of approximately 18.9kDa.
G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

G-CSF Lyophilized from 10mM NaCitrate, pH 4.0 and 150mM NaCl.

Solubility

It is recommended to reconstitute the lyophilized Granulocyte Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Granulocyte Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Amino acid sequence

VPLVTVSAL PPSLPLPRSF LLKSLEQVRK IQASGSVLLE QLCATYKLCH PEELVLLGHS LGIPKASLSG CSSQALQQTQ CLSQLHSGLC LYQGLLQALS GISPALAPTL DLLQLDVANF ATTIWQQMEN LGVAPTVQPT QSAMPAFTSA FQRRAGGVLA ISYLQGFLET ARLALHHLA.

Purity

Greater than 98.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Biological Activity

The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 2 x 107IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-GCSF Monkey

  • Description

  • GCSF Monkey

  • Granulocyte Colony Stimulating Factor Recombinant Rhesus Macaque
  • CYT-1121

Catalogue number

CYT-1121

Synonyms

CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.

Introduction

GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. 3 transcript variants encoding 3 different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that take part in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

Description

Granulocyte Colony Stimulating Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of approximately 18.9kDa.
GCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4.

Solubility

It is recommended to reconstitute the lyophilized Granulocyte Colony Stimulating Rhesus Macaque in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulocyte Colony Stimulating Rhesus Macaque should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.

Biological Activity

The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is <   0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-GCSF Rat

  • Description

  • GCSF Rat

  • Granulocyte-Colony Stimulating Factor Rat Recombinant
  • CYT-940

Catalogue number

CYT-940

Synonyms

Granulocyte colony stimulating factor, Protein Csf3, Csf3.

Introduction

GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

Description

GCSF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.5kDa.
The G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a 0.2µm filtered solution in 5mM Sodium Citrate, pH 4.0.

Solubility

It is recommended to reconstitute the lyophilized GCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized G-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 97.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.

Biological Activity

The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.

Usage

ProSpec’s products are furnished forLABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-GM CSF Human

  • Description

  • GM CSF Human

  • Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant
  • CYT-221

Catalogue number

CYT-221

Synonyms

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

Introduction

Granulocyte Macrophage Colony Stimulating Factor was first characterized as a growth factor that supports the in-vitro colony formation of granulocytes-macrophages progenitor cells. It is a pleiotropic cytokine and a member of a family of endogenous cytokines of the hematopoietic system. GM-CSF is produced as a response to immune or inflammatory stimuli by activated cells of the hematopoietic system such as T cells, B cells, macrophages, mast cells and also fibroblasts and alveolar epithelial cells. It plays an important role in regulating the proliferation, differentiation, survival and activation of hematopoietic cells such as granulocytes and monocytes ,neutrophiles, basophiles and eosonophoiles, erythroid cells, megakaryocytes and T cells.
Human and mouse GM-CSF have about 56% homology and are species specific. Human GM-CSF is not active on mouse cells and vice versa. It is active on canine and feline cells.
GMCSF is 144 amino acids, 22kDa glycoprotein. It is composed of four bundles alpha helices. Its receptor is heterodimers with a ligand-specific alpha subunit and a betac subunit that is shared with the interleukin IL-3 and IL-5 receptors. This unusual form of receptor assembly likely applies also to IL-3 and IL-5 receptors. Cross-linking the two receptor subunits is required for receptor activation and signaling .
GMCSF has been shown to be involved in maturation, mobilization and antigen presentation of myeloid dentritic cells in-vivo or ex-vivo. This function promotes Th1 immune responses, cytotoxcity, anti-angiogenesis as well as allergic inflammation, and the development of autoimmunity. Therefore GMCSF can be used in immunotherapy for the treatment of immune suppressed and immune-compromised patients as well as in veterinary medicine for the same purpose. GM-CSF is also important in regulation of embryo development and pregnancy and specifically in embryo implantation and subsequent development .

Description

Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14477 Dalton. GM-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

GM-CSF was lyophilized after extensive dialysis against 2mM sodium phosphate buffer pH= 7.4±0.1.

Solubility

It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by:
1. Analysis by RP-HPLC.
2. Analysis by -PAGE.

Amino acid sequence

The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
N-terminal methionine has been completely removed enzymatically.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 11,100,000 IU/mg.

Protein content

GM-CSF quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.963 as the extinction coefficient for a 0.1% solution. This value is calculated by the PC GEN computer analysis program of protein sequences .
2. Analysis by RP-HPLC, using a standard solution of GM-CSF as a Reference Standard.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Background

GM-CSF has similar effects to G-CSF which is widely used as a therapeutic agent in immunosupressed patients mostly to boost production of the myeloid lineage after chemotherapy-induced neutropenia. Using GM-CSF was also shown to boost anti-tumor immunity by promoting the maturation of antigen presenting dendritic cells and Th1 responses. It was suggested for therapeutic uses in various cancers including follicular lymphoma, acute leukemia and prostate cancer. GM-CSF is particular affective as an antitumor vaccine when used in tumor cells engineered to secret GM-CSF. GM-CSF is also involved in the treatment of Crohn’s disease. Another use of GM-CSF is as a vaccine adjuvant and it was also claimed to improve the general health condition of AIDS patients although this is a controversial issue and it was recently found that GM-CSF actually induces the expression of HIV-1in monocytes.  GM-CSF was also found to be effective and is used in veterinary medicine. 

GM-CSF was also shown to play a pivotal role in regulation of embryo development and pregnancy and particularly in embryo implantation and placenta development. 

Abnormalities in GM-CSF production or receptor function were implicated in diseases such rheumatoid arthritis, juvenile and chronic myelomonocytic leukemia and alveolar proteinosis as well as in the pathogenesis of myeloproliferative diseases.

 

 

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ProSpec-GM CSF Human, His

  • Description

  • GM CSF Human, His

  • Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, His Tag
  • CYT-477

Catalogue number

CYT-477

Synonyms

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

Introduction

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. Granulocyte Macrophage Colony Stimulating Factor is a potent species-specific growth factor produced by a variety of cell types including T cells, B cells, macrophages, mast cells and endothelial cells. GM-CSF is produced in response to cytokine or immune stimulation and has been shown to stimulate the proliferation, maturation and function of hematopoietic cells.

Description

GMCSF Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids fragment and having a molecular mass of 18.98kDa with an amino-terminal hexahistidine tag.
GM-CSF Human Recombinant His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

Granulocyte Macrophage Colony Stimulating Factor-His is supplied in 20mM Tris HCl and 50% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
Please avoid freeze thaw cycles.

Purity

Greater than 95.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-GM CSF Human, Pichia

  • Description

  • GM CSF Human, Pichia

  • Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Pichia
  • CYT-324

Catalogue number

CYT-324

Synonyms

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

Introduction

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

Description

Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in Yeast is a single, glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 26-32 kDa. rhGMCSF differs from the natural human GM-CSF by a substitution of leucine at position 23 , and the carbohydrate moiety may be different from the native protein.
GM-CSF is purified by proprietary chromatographic techniques.

Source

Pichia Pastoris.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution containing 10mM phosphate buffer pH 7.0, 40 mg mannitol and 10 mg sucrose.

Solubility

It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 97.0% as determined by1. Analysis by RP-HPLC.
2. Analysis by -PAGE.

Amino acid sequence

The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-GM CSF Human, Sf9

  • Description

  • GM CSF Human, Sf9

  • Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Sf9
  • CYT-416

Catalogue number

CYT-416

Synonyms

CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

Introduction

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

Description

GM-CSF Human Recombinant produced in insect cells is a single, glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.6kDa.
GM-CSF is fused to a C-terminal His -tag and purified by proprietary chromatographic techniques.

Source

Insect Cells.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized with PBS.

Solubility

It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by -PAGE.

Amino acid sequence

The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs,agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-GM CSF K9

  • Description

  • GM CSF K9

  • Granulocyte Macrophage-Colony Stimulating Factor Canine Recombinant
  • CYT-724

Catalogue number

CYT-724

Synonyms

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

Introduction

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

Description

GMCSF k9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14.2 kDa. GM-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

GMCSF was lyophilized after extensive dialysis against 1xPBS pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 96.0% as determined by
1. Analysis by RP-HPLC.
2. Analysis by -PAGE.

Amino acid sequence

APTRSPTLVT RPSQHVDAIQ EALSLLNNSN DVTAVMNKAV KVVSEVFDPE
GPTCLETRLQ LYKEGLQGSL TSLKNPLTMM ANHYKQHCPP TPESPCATQN
INFKSFKENL KDFLFNIPFD CWKPVKK.

Biological Activity

The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF1 erythroleukemic cells is typically 1-4 ng/ml.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-GM CSF Monkey

  • Description

  • GM CSF Monkey

  • Granulocyte Macrophage-Colony Stimulating Factor Rhesus Macaque Recombinant
  • CYT-720

Catalogue number

CYT-720

Synonyms

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

Introduction

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13. GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

Description

Granulocyte Macrophage Colony Stimulating Factor Monkey Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.4 kDa.
GM-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

GM-CSF was lyophilized from a concentrated solution containing 1x PBS pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein . Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by -PAGE and RP-HPLC.

Amino acid sequence

APARSPSPGT QPWEHVNAIQ EARRLLNLSR DTAAEMNKTV EVVSEMFDLQ EPSCLQTRLE LYKQGLQGSL TKLKGPLTMM ASHYKQHCPP TPETSCATQI ITFQSFKENL KDFLLVIPFD CWEPVQE.

Biological Activity

The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-GM CSF Mouse

  • Description

  • GM CSF Mouse

  • Granulocyte Macrophage-Colony Stimulating Factor Mouse Recombinant
  • CYT-222

Catalogue number

CYT-222

Synonyms

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF

Introduction

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

Description

Granulocyte Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids and having a molecular mass of 14285.35 Dalton.
GM-CSF Mouse is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

GM-CSF Mouse was lyophilized with no additives.

Solubility

It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 20mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GM-CSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

Protein content

GM-CSF quantitation was carried out by two independent methods
1. UV spectroscopy at 280 nm using the absorbency value of 0.765 as the extinction coefficient for a 0.1% solution. This value is calculated by the PC GENE computer analysis program of protein sequences .

2. Analysis by RP-HPLC, using a calibrated solution of GM-CSF as a Reference Standard.

References

1.Title:Multigene/multisubtype HIV-1 vaccine induces potent cellular and humoral immune responses by needle-free intradermal delivery.
Publication: Mol Ther. 2005 Dec;12:1197-205. Epub 2005 Aug 22. PMID: 16112909
Link: http://www.nature.com/mt/journal/v12/n6/full/mt20051405a.html
Applications: The Mouse GM-CSF used for 2 purposes:
1. As an adjuvant for DNA vaccine which included seven plasmids encoding nine HIV-1 proteins. The mice were injected with the DNA vaccine together with recombinant mouse GM-CSF. 2. Used in Elisa.

2.Title: Neospora caninum: cloning and expression of a gene coding for cytokine-inducing profilin. 
Publication: Exp Parasitol. 2010 Aug;125:357-62. Epub 2010 Mar 6. PMID: 20211619
Link: http://www.sciencedirect.com/science/article/pii/S001448941000086X
Applications: Used for immunoblotting

3.Title: Intranasal Granulocyte-Macrophage Colony-Stimulating Factor Reduces the Aspergillus Burden in an Immunosuppressed Murine Model of Pulmonary Aspergillosis.
Publication: Antimicrob Agents Chemother. 2008 February; 52: 716–718.
Published online 2007 November 5
Link: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2224773/?tool=pmcentrez
Applications: GM-CSF as tested a therapeutic potential in a murine model of pulmonary aspergillosis. In summary, this pilot study indicates that GM-CSF administered intranasally may be a novel therapeutic approach for the prevention or treatment of pulmonary fungal infections and may augment the efficacies of antifungal agents.
GM-CSF was given intranasal.

4.Title: Dendritic Cell-Based Therapeutic Vaccination against Myeloma: Vaccine Formulation Determines Efficacy against Light Chain Myeloma
Publication: The Journal of Immunology February 1, 2009 vol. 182 no. 3 1667-1673
Link:
http://www.jimmunol.org/content/182/3/1667.full

5.Title:Pre-clinical Evaluation of a CEA DNA Prime/protein Boost Vaccination Strategy Against Colorectal Cancer.
Publication:Article first published online: 21 JUN 2007 DOI:10.1111/j.1365-3083.2007.01945.x

Scandinavian Journal of Immunology Volume 66, Issue 1, pages 43–51, July 2007
Link:http://onlinelibrary.wiley.com/doi/10.1111/j.1365-3083.2007.01945.x/full

6.Title:Intranasal Granulocyte-Macrophage Colony-Stimulating Factor Reduces the Aspergillus Burden in an Immunosuppressed Murine Model of Pulmonary Aspergillosis.
Publication: First published November 2007, doi: 10.1128/?AAC.00760-07 Antimicrob. Agents Chemother. February 2008 vol. 52 no. 2 716-718
Link:http://aac.asm.org/content/52/2/716.full

7. Title: O-glycosylated versus non-glycosylated MUC1-derived peptides as potential targets for cytotoxic immunotherapy of carcinoma.
Publications:  Clinical & Experimental Immunology 143.1 : 139-149.
Link: http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2249.2005.02965.x/epdf
8. Title: Novel Functions of Herbal Medicines in DendriticCells: Role of Amomi Semen in Tumor Immunity
Publications:  Microbiology and immunology 51.11 : 1121-1133.
Link: http://onlinelibrary.wiley.com/doi/10.1111/j.1348-0421.2007.tb03998.x/epdf
9. Title: The Herbal Medicine Compound Falcarindiol from Notopterygii Rhizoma Suppresses Dendritic Cell Maturation
Publication:  Journal of Pharmacology and Experimental Therapeutics 333.3 : 954-960.
Link: http://jpet.aspetjournals.org/content/333/3/954.full

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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  • GM CSF Human, Pichia
  • GMCSF Porcine
  • GMCSF Poricne, His

ProSpec-GM CSF Rat

  • Description

  • GM CSF Rat

  • Granulocyte Macrophage-Colony Stimulating Factor Rat Recombinant
  • CYT-395

Catalogue number

CYT-395

Synonyms

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

Introduction

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

Description

Granulocyte Macrophage Colony Stimulating Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14590.65 Dalton. GM-CSF Rat Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

GM-CSF Rat was lyophilized with no additives.

Solubility

It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 96.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI

QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE

VTTFEDFIKN LKGFLFDIPF DCWKPVQK.

Biological Activity

The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.

Usage

ProSpec’s products are furnished forLABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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  • GMCSF Porcine

ProSpec-GMCSF Porcine

  • Description

  • GMCSF Porcine

  • Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant
  • CYT-1095

Catalogue number

CYT-1095

Synonyms

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

Introduction

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of GMCSF is found extracellularly as a homodimer. GMCSF has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

Description

Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant produced in E. coli is a non-glycosylated monomer chain containing 128 amino acids and having a  molecular mass of 14.5kDa.

GMCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a sterile filtered solution containing 10mM sodium phosphate, pH 7.5.

Solubility

It is recommended to reconstitute the lyophilized GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C.

Please prevent freeze-thaw cycles.

Amino acid sequence

MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK.

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

The ED50, as determined by TF-1 cell proliferation is 4.52ng/ml corresponding to a specific activity which is 2.2 x 10^5 units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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  • GM CSF Rat
  • GMCSF Poricne, His

ProSpec-GMCSF Poricne, His

  • Description

  • GMCSF Poricne, His

  • Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant, His Tag
  • CYT-1160

Catalogue number

CYT-1160

Synonyms

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim

Introduction

The hematopoietic growth factor GM-CSF or granulocyte macrophage colony-stimulating factor, stimulates the development of neutrophils & macrophages, enhance proliferation and development of early erythroid megakaryocytic & eosinophilic progenitor cells. GM-CSF is secreted from the fibroblasts, monocytes, T-lymphocytes & endothelial cells. This protein blocks the migration of neutrophils & induces the biological activity of mature end-cells.

Description

GMCSF Poricne Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids and having a molecular mass of 16.6kDa.
GMCSF is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

GMCSF protein solution containing Phosphate-Buffered Saline .

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-M CSF Human

  • Description

  • M CSF Human

  • Macrophage-Colony Stimulating Factor Human Recombinant
  • CYT-308

Catalogue number

CYT-308

Synonyms

Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

Introduction

Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

Description

Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 159 amino acids and having a total molecular mass of 37.1 KD. MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The MCSF protein was lyophilized with 10mM sodium Phosphate, pH-8.0 & 50mM NaCl.

Solubility

It is recommended to reconstitute the lyophilized MCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles.

Amino acid sequence

MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ GHERQSEGS.

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

The ED50, calculated by the dose-dependent stimulation of the proliferation of murine M-NFS-60 indicator cells was found to be 1.15ng/ml corresponding to a specific activity of 8.7×105 Units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

References

1.Title:Osteoclasts Control Osteoblast Chemotaxis via PDGF-BB/PDGF Receptor Beta Signaling.
Publication:Sanchez-Fernandez MA, Gallois A, Riedl T, Jurdic P, Hoflack B Osteoclasts Control Osteoblast Chemotaxis via PDGF-BB/PDGF Receptor Beta Signaling. PLoS ONE 3: e3537. doi:10.1371/journal.pone.0003537.
Link:http://www.plosone.org/article/info:doi%2F10.1371%2Fjournal.pone.0003537#references

2.Title:Suppressor of cytokine signalling-3 at pathological levels does not regulate lipopolysaccharide or interleukin-10 control of tumour necrosis factor-? production by human monocytes.
Publication:Article first published online: 11 MAY 2006 DOI: 10.1111/j.1365-2567.2006.02383.x
Link:http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2567.2006.02383.x/full

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ProSpec-M CSF Human, Baculovirus

  • Description

  • M CSF Human, Baculovirus

  • Macrophage Colony Stimulating Factor Human Recombinant, Baculovirus
  • CYT-637

Catalogue number

CYT-637

Synonyms

CSF-1, Lanimostim, MCSF, MGC31930, M-CSF, Macrophage colony-stimulating factor 1, CSF1.

Introduction

Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

Description

Macrophage Colony Stimulating Factor Human Recombinant produced in Baculovirus is a disulfide linked homodimer, glycosylated, polypeptide chain containing 2 x 149 amino acids and having a total molecular mass of 42 kDa.
MCSF is purified by proprietary chromatographic techniques.

Source

Baculovirus infected Silkworm.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The lyophilized protein was lyophilized with 20mM phosphate buffer, 1% HSA and 3% manntiol.

Solubility

It is recommended to reconstitute the lyophilized M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles.

Amino acid sequence

EEVSEYCSHM IGSGHLQSLQ RLIDSQMETS CQITFEFVDQ EQLKDPVCYL KKAFLLVQDI MEDTMRFRDN TPNAIAIVQL QELSLRLKSC FTKDYEEHDK ACVRTFYETP LQLLEKVKNV FNETKNLLDK DWNIFSKNCN NSFAECSSQ.

Purity

Greater than 95.0% as determined by Analysis by RP-HPLC.
Analysis by -PAGE.

Biological Activity

The ED50, calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells was found < 3ng/ml, corresponding to a specific activity of less than 333,333.33units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-M CSF Human, HEK

  • Description

  • M CSF Human, HEK

  • Macrophage Colony Stimulating Factor Human Recombinant, HEK
  • CYT-106

Catalogue number

CYT-106

Synonyms

Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

Introduction

Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

Description

M-CSF Human Recombinant produced in HEK cells is a glycosylated homodimer, having a molecular weight range of 35-40kDa due to glycosylation.
The M-CSF is purified by proprietary chromatographic techniques.

Source

HEK.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The M-CSF was lyophilized from a 0.2µm filtered solution containing 0.67mg/ml in 1xPBS.

Solubility

It is recommended to reconstitute the lyophilized M-CSF in sterile 1xPBS containing 0.1% endotoxin-free recombinant HSA.

Stability

Lyophilized M-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution M-CSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95% as obsereved by -PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells and is 1.13ng/ml.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-M CSF Human, His

  • Description

  • M CSF Human, His

  • Macrophage Colony Stimulating Factor Human Recombinant, His Tag
  • CYT-695

Catalogue number

CYT-695

Synonyms

CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

Introduction

Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

Description

Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 179 amino acids and having a total molecular mass of 20.7 kDa.
MCSF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile filtered colorless solution.

Formulation

The MCSF protein solution contains 20mM Tris-HCl, pH-8, 2mM DTT & 10% Glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ DVVTKPDCN.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-M CSF Human, Sf9 His

  • Description

  • M CSF Human, Sf9 His

  • Macrophage Colony Stimulating Factor Human Recombinant, Sf9
  • CYT-1015

Catalogue number

CYT-1015

Synonyms

Macrophage colony-stimulating factor 1, CSF-1, M-CSF, MCSF, Lanimostim.  

Introduction

Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

Description

MCSF produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 231 amino acids and having a molecular mass of 26.1kDa .
MCSF is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

MCSF protein solution contains Phosphate Buffered Saline and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

Measured in a cell proliferation assay using M-NFS-60 mouse myelogenous leukemia lymphoblast cell. The ED50 for this effect is less or equal to 3 ng/ml.

Amino acid sequence

EEVSEYCSHM IGSGHLQSLQ RLIDSQMETS CQITFEFVDQ EQLKDPVCYL KKAFLLVQDI MEDTMRFRDN TPNAIAIVQL QELSLRLKSC FTKDYEEHDK ACVRTFYETP LQLLEKVKNV FNETKNLLDK DWNIFSKNCN NSFAECSSQD VVTKPDCNCL YPKAIPSSDP ASVSPHQPLA PSMAPVAGLT WEDSEGTEGS SLLPGEQPLH TVDPGSAKQR PPRLEHHHHH H.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-M CSF Mouse

  • Description

  • M CSF Mouse

  • Macrophage-Colony Stimulating Factor Mouse Recombinant
  • CYT-439

Catalogue number

CYT-439

Synonyms

CSF-1, Lanimostim, MCSF, M-CSF.

Introduction

Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

Description

Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 156 amino acids and having a total molecular mass of 36.4 KD.
MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a sterile filtered solution containing 10mM sodium phosphate, 50mM sodium chloride, pH 7.5.

Solubility

It is recommended to reconstitute the lyophilized M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized M-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles.

Amino acid sequence

MKEVSEHCSH MIGNGHLKVL QQLIDSQMET SCQIAFEFVD QEQLDDPVCY LKKAFFLVQD IIDETMRFKD NTPNANATER LQELSNNLNS CFTKDYEEQN KACVRTFHET PLQLLEKIKN FFNETKNLLE KDWNIFTKNC NNSFAKCSSR DVVTKP.

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

The ED50, as calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells is 1.33ng/ml corresponding to a specific activity of 7.5×105 units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-M CSF Rat

  • Description

  • M CSF Rat

  • Macrophage-Colony Stimulating Factor Rat Recombinant
  • CYT-856

Catalogue number

CYT-856

Synonyms

Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, Csfm.

Introduction

Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

Description

Macrophage Colony Stimulating Factor Rat Recombinant produced in E.coli is a non-glycosylated homodimer, containing 2 x 155 amino acids and having a total molecular mass of 36.2 kDa.
MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a sterile filtered aqueous solution containing 10mM Na3PO4, pH 7.5.

Solubility

It is recommended to reconstitute the lyophilized MCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Amino acid sequence

MEVSEHCSHM IGNGHLQILQ QLIDSQMETA CLIEYKFVDQ EQLDDPVCYL KKAFVLVQVI IEETMRFKDN TPNANATERL QELSMKLNSC FIKDYKEQNE ACVQTYKESP LRLLEKIKNF  FNETKNFLEK DWNIFSKNCN DSLAKCSSRD VVTKP.

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

The activity as determined by dose-dependent induction of M-NFS-60 cell proliferation is 1.65 ng/ml. This corresponds to an expected specific activity of 6.1×105 units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-M CSF Rat HEK

  • Description

  • M CSF Rat HEK

  • Macrophage Colony Stimulating Factor Rat Recombinant HEK
  • CYT-046

Catalogue number

CYT-046

Synonyms

CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

Introduction

Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

Description

MCSF Rat Recombinant produced in HEK-293 cells is a secreted protein . M-CSF is disulfide-linked homodimer containing 2 x 222 a.a chains.

Source

HEK293

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The recombinant MCSF was lyophilized after extensive dialysis against PBS.

Solubility

It is recommended to reconstitute the MCSF in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of mouse M-NFS-60 cells.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-MCSF Mouse, Sf9

  • Description

  • MCSF Mouse, Sf9

  • Macrophage Colony Stimulating Factor Mouse Recombinant, Sf9
  • CYT-1141

Catalogue number

CYT-1141

Synonyms

M-Csf, Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, C87615, MCSF, op, Processedmacrophage colony-stimulating factor 1.

Introduction

Macrophage Colony Stimulating Factor or colony stimulating factor 1, is a cytokine, that  promoted differentiation in hematopoietic stem cells to  macrophages. Another role of M CSF is to bind to its receptor and to  take part in placenta growth and development.

Description

MCSF Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 164 amino acids and having a molecular mass of 19.1 kDa.
MCSF is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

The MCSF solution contains 10% Glycerol and Phosphate-Buffered Saline .

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 90.0% as determined by -PAGE.

Biological Activity

Determined by cell proliferation assay using M-NFS-60 mouse myelogenous leukemia lymphoblast cells. ED50 range for this effect is ≤ 4ng/ml.

Amino acid sequence

ADPKEVSEHC SHMIGNGHLK VLQQLIDSQM ETSCQIAFEF VDQEQLDDPV CYLKKAFFLV
QDIIDETMRF KDNTPNANAT ERLQELSNNL NSCFTKDYEE QNKACVRTFH ETPLQLLEKI
KNFFNETKNL LEKDWNIFTK NCNNSFAKCS SRDVVTKPHH HHHH

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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  • M CSF Human
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  • M CSF Human, HEK

ProSpec-MCSFR Human

  • Description

  • MCSFR Human

  • Colony Stimulating Factor 1 Receptor Human Recombinant
  • CYT-1068

Catalogue number

CYT-1068

Synonyms

Macrophage colony-stimulating factor 1 receptor, CSF-1 receptor , CSF-1-R, CSF-1R, M-CSF-R, Proto-oncogene c-Fms, CD115, CSF1R, FMS. 

Introduction

MCSFR which is also familiar as CSF1R, is part of the type3 subfamily of receptor tyrosine kinases. MCSFR is expressed mainly on cells of the monocyte and macrophage lineage, stem cells, and in the growing placenta. Most of the biological effects of this cytokine are mediated by MCSFR. MCSFR contains an extracellular ligand-binding domain, a single membrane-spanning segment, and an intracellular tyrosine kinase domain. Originally CSF1 and this receptor were implicated as vital for normal trophoblastic implantation as well as monocyte development. The role of CSF1/CSF1R in normal mammary gland development is actually very interesting since this connection has also been discovered in the biology of breast cancer with the results of abnormal expression of CSF1 and its receptor. Likewise, in Alzheimer’s disease and after brain injuries an increased level of CSF1R was found in the microglia, which causes the microglia to become more active.

Description

MCSFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 737 amino acids and having a molecular mass of 82.1kDa. .
MCSFR is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

MCSFR protein solution contains Phosphate Buffered Saline and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 90.0% as determined by -PAGE.

Biological Activity

Measured by its ability to inhibit M-CSF dependent proliferation of M-NFS-60 mouse myelogenous leukemia lymphoblast cells. The ED50 for this effect is less or equal to 100ng/ml in the presence of 10 ng/ml M-CSF.

Amino acid sequence

IPVIEPSVPE LVVKPGATVT LRCVGNGSVE WDGPPSPHWT LYSDGSSSIL STNNATFQNT GTYRCTEPGD PLGGSAAIHL YVKDPARPWN VLAQEVVVFE DQDALLPCLL TDPVLEAGVS LVRVRGRPLM RHTNYSFSPW HGFTIHRAKF IQSQDYQCSA LMGGRKVMSI SIRLKVQKVI PGPPALTLVP AELVRIRGEA AQIVCSASSV DVNFDVFLQH NNTKLAIPQQ SDFHNNRYQK VLTLNLDQVD FQHAGNYSCV ASNVQGKHST SMFFRVVESA YLNLSSEQNL IQEVTVGEGL NLKVMVEAYP GLQGFNWTYL GPFSDHQPEP KLANATTKDT YRHTFTLSLP RLKPSEAGRY SFLARNPGGW RALTFELTLR YPPEVSVIWT FINGSGTLLC AASGYPQPNV TWLQCSGHTD RCDEAQVLQV WDDPYPEVLS QEPFHKVTVQ SLLTVETLEH NQTYECRAHN SVGSGSWAFI PISAGAHTHP PDEFLFTPLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-CTGF (182-250 a.a.) Human

  • Description

  • CTGF Human

  • Connective Tissue Growth Factor Human Recombinant
  • CYT-526

Catalogue number

CYT-526

Synonyms

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Introduction

Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 , CTGF , Nov , WISP-1, 2 and 3 . The CCN genes encode secreted proteins associated with the Extracellular Matrix and cell membrane. CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes. The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins .
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion. Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand’s factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain. Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy. In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

Description

The Connective Tissue Growth Factor amino acids 182-250, produced in E.Coli, is a fusion protein with His Tag , having a total molecular mass of 15 kDa.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered white lyophilized powder.

Formulation

Lyophilized without any additives.

Solubility

It is recommended to reconstitute the lyophilized CTGF in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized CTGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTGF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long-term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 90.0% as determined by -PAGE.

Usage

Prospec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-CTGF Human

  • Description

  • CTGF Human

  • Connective Tissue Growth Factor Human Recombinant
  • CYT-541

Catalogue number

CYT-541

Synonyms

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Introduction

Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 , CTGF , Nov , WISP-1, 2 and 3 . The CCN genes encode secreted proteins associated with the Extracellular Matrix and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the IGFBPs.
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand’s factor and mucins. Sequence similarities to binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

Description

CTGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.2 kDa.
The CTGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

CTGF was Lyophilized from a sterile filtered aqueous solution containing 0.1% Trifluoroacetic Acid .

Solubility

It is recommended to reconstitute the lyophilized CTGF in sterile 18MΩcm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. 

Stability

Lyophilized CTGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTGF should be stored at 4°C between 2-7 days and for future use below -18°C.

For long term storage it is recommended to add a carrier protein .

Please prevent freeze-thaw cycles. 

Purity

Purity of CTGF is greater than 90% as determined by -PAGE.

Biological Activity

Determined by the dose-dependent stimulation of the proliferation of HUVEC cells. The expected ED50 for this effect is 1-2µg/ml, corresponding to a specific activity of 500-1000units/mg.

Amino acid sequence

MGKKCIRTPK ISKPIKFELS GCTSMKTYRA KFCGVCTDGR CCTPHRTTTL PVEFKCPDGE VMKKNMMFIK TCACHYNCPG DNDIFESLYY RKMYGDMA.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-CTGF Human (183-255)

  • Description

  • CTGF Human

  • Connective Tissue Growth Factor Human Recombinant
  • CYT-1174

Catalogue number

CYT-1174

Synonyms

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Introduction

Connective Tissue Growth Factor is a part of the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 , CTGF, Nov , WISP-1, 2 and 3 . CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: tumorigenesis,fibrosis and vascular ailments. Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of 4 modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins .
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

Description

CTGF Human Recombinant is a single, glycosylated polypeptide chain containing 80 amino acids and having a molecular mass of 9.1kDa . CTGF is fused to a 7 a.a His tag at N-terminal.

Source

HEK293 cells.

Physical Appearance

Filtered White lyophilized powder.

Formulation

CTGF filtered and lyophilized from 0.5mg/ml in 20 mM Tris buffer and 50 mM NaCl, pH 7.5.

Solubility

It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

Stability

Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

MHHHHHHRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK. 

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-CTGF Human, HEK

  • Description

  • CTGF Human, HEK

  • Connective Tissue Growth Factor Human Recombinant , HEK
  • CYT-687

Catalogue number

CYT-687

Synonyms

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.

Introduction

Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 , CTGF , Nov , WISP-1, 2 and 3 . The CCN genes encode secreted proteins associated with the Extracellular Matrix and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins .
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand’s factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

Description

The CTGF Human Recombinant produced in HEK293 cells, is 36kDa protein containing a total of 329 amino acid residues including a C-terminal 6×His tag.

Source

HEK293 cells.

Physical Appearance

Filtered colorless solution.

Formulation

CTGF filtered solution in 0.1M Citrate buffer pH 4.7 and 20% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Amino acid sequence

QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.

Purity

Greater than 90.0% as determined by -PAGE.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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  • CTGF Human
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  • CTGF Human, His
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ProSpec-CTGF Human, His

  • Description

  • CTGF Human, His

  • Connective Tissue Growth Factor Human Recombinant, His Tag
  • CYT-438

Catalogue number

CYT-438

Synonyms

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Introduction

Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 , CTGF , Nov , WISP-1, 2 and 3 . The CCN genes encode secreted proteins associated with the Extracellular Matrix and cell membrane. CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes. The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins .
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion. Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand’s factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy. In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells. CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

Description

CTGF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids and having a molecular mass of 37.7kDa.
The CTGF is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

CTGF protein is supplied in 20mM Tris-HCl, pH-8 and 10% Glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 85.0% as determined by Analysis by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MQNCSGPCRC PDEPAPRCPA GVSLVLDGCG CCRVCAKQLG ELCTERDPCD PHKGLFCDFG SPANRKIGVC TAKDGAPCIF GGTVYRSGES FQSSCKYQCT CLDGAVGCMP LCSMDVRLPS PDCPFPRRVK LPGKCCEEWV CDEPKDQTVV GPALAAYRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK CIRTPKISKP IKFELSGCTS MKTYRAKFCG VCTDGRCCTP HRTTTLPVEF KCPDGEVMKK NMMFIKTCAC HYNCPGDNDI FESLYYRKMY GDMA.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Related Products

  • CTGF Human, HEK
  • CTGF Human
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  • CTGF Human

ProSpec-CTGF Mouse

  • Description

  • CTGF Mouse

  • Connective Tissue Growth Factor Mouse Recombinant
  • CYT-1173

Catalogue number

CYT-1173

Synonyms

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Introduction

Connective Tissue Growth Factor is a part of the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 , CTGF, Nov , WISP-1, 2 and 3 . CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: tumorigenesis,fibrosis and vascular ailments. Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of 4 modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins .
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

Description

CTGF Mouse Recombinant is a single, glycosylated polypeptide chain containing 329 amino acids and having a molecular mass of 36.2kDa . CTGF is fused to a 6 a.a His tag at C-terminal.

Source

HEK293

Physical Appearance

Filtered clear solution.

Formulation

CTGF protein solution is filtered in in 0.1M citrate buffer pH 4,7 and 20% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
Avoid multiple freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

QDCSAQCQCA AEAAPHCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCDFGS PANRKIGVCT AKDGAPCVFG GSVYRSGESF QSSCKYQCTC LDGAVGCVPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDRTAVG PALAAYRLED TFGPDPTMMR ANCLVQTTEW
SACSKTCGMG ISTRVTNDNT FCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKIAKPV KFELSGCTSV KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEIMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMAHHHHHH

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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ProSpec-MFGE8 Mouse

  • Description

  • MFGE8 Mouse

  • Milk Fat Globule-EGF Factor 8 Protein Mouse Recombinant
  • CYT-1000

Catalogue number

CYT-1000

Synonyms

Milk fat globule-EGF factor 8 protein, isoform CRA_a, Putative uncharacterized protein, Mfge8, mCG_6301.

Introduction

Milk fat globule-EGF factor 8 protein is pleiotropic secreted glycoprotein which promotes mammary gland morphogenesis, angiogenesis, and tumor progression. Mfge8 has also an imperative role in tissue homeostasis and the prevention of inflammation. Mfge8 functions as a bridge between phosphatidylserine on apoptotic cells and Integrin alpha V beta 3 on phagocytes, leading to the clearance of apoptotic debris.

Description

MFGE8 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids and having a molecular mass of 46kDa .
MFGE8 is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

MFGE8 protein solution contains Phosphate Buffered Saline and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

ADLASGDFCD SSLCLNGGTC LTGQDNDIYC LCPEGFTGLV CNETERGPCS PNPCYNDAKC LVTLDTQRGD IFTEYICQCP VGYSGIHCET GCSTQLGMEG GAIADSQISA SSVYMGFMGL QRWGPELARL YRTGIVNAWT ASNYDSKPWI QVNLLRKMRV SGVMTQGASR AGRAEYLKTF KVAYSLDGRK FEFIQDESGG DKEFLGNLDN NSLKVNMFNP TLEAQYIKLY PVSCHRGCTL RFELLGCELH GCSEPLGLKN NTIPDSQMSA SSSYKTWNLR AFGWYPHLGR LDNQGKINAW TAQSNSAKEW LQVDLGTQRQ VTGIITQGAR DFGHIQYVAS YKVAHSDDGV QWTVYEEQGS SKVFQGNLDN NSHKKNIFEK PFMARYVRVL PVSWHNRITL RLELLGCHHH HHH.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF (1-51), Human

  • Description

  • EGF , Human

  • Epidermal Growth Factor Human Recombinant
  • CYT-1115

Catalogue number

CYT-1115

Synonyms

Urogastrone, URG, EGF.

Introduction

Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of several epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

Description

Epidermal Growth Factor Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 6.0kDa. The EGF is purified by proprietary chromatographic techniques. 

Source

Saccharomyces cerevisiae

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. 

Stability

Lyophilized EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epidermal Growth Factor should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

NECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

Biological Activity

The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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