ProSpec-GRO b Human His CHM-356,GRO-Beta Human Recombinant , His Tag

ProSpec-GRO b Human His CHM-356,GRO-Beta Human Recombinant , His Tag,CXCL2 的基因位于人类 4 号染色体上的其他 CXC 趋化因子簇中。 CXCL2 通过与称为 CXCR2 的细胞表面趋化因子受体相互作用来动员细胞。

    • GRO b Human, His

    • GRO-Beta Human Recombinant , His Tag
    • CHM-356

Catalogue number

CHM-356

Synonyms

Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

Introduction

趋化因子配体 2 是属于 CXC 趋化因子家族的一种小细胞因子,也称为巨噬细胞炎症蛋白 2-α、生长调节蛋白 β 和 Gro oncogene-2。 CXCL2 在氨基酸序列上与相关趋化因子 CXCL1 有 90% 相同。 这种趋化因子由单核细胞和巨噬细胞分泌,对多形核白细胞和造血干细胞具有趋化作用。 CXCL2 的基因位于人类 4 号染色体上的其他 CXC 趋化因子簇中。 CXCL2 通过与称为 CXCR2 的细胞表面趋化因子受体相互作用来动员细胞。

Description

GRO-Beta Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 94 amino acids and having a molecular mass of 10.1 kDa. The GRO-b 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 Human CXCL2 protein solution contains 20mM Tris HCl .

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 MAPLATELRC QCLQTLQGIH LKNIQSVKVK SPGPHCAQTE VIATLKNGQK ACLNPASPMV KKIIEKMLKNGKSN.

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-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.

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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, 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-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-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-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, 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-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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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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  • CTGF Human, His
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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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  • CTGF Human
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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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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.

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  • CTGF Human, HEK
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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-EGF Mouse, His

  • Description
  • EGF Mouse, His

  • Epidermal Growth Factor Mouse Recombinant, His Tag
  • CYT-138

Catalogue number

CYT-138

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 various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

Description

EGF mouse Recombinant produced in E. coli is a single polypeptide chain containing 77 amino acids and having a molecular mass of 8.6kDa.
EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

The EGF solution contains 20mM Tris-HCl buffer , 100mM NaCl, 2mM DTT 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% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

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-EGFL6 Mouse

  • Description
  • EGFL6 Mouse

  • EGF Like Domain Multiple 6 Mouse Recombinant
  • CYT-1105

Catalogue number

CYT-1105

Synonyms

Epidermal growth factor-like protein 6, EGF-L6, Egfl6, Maeg.

Introduction

Epidermal Growth Factor­like Domain Multiple 6 belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.

Description

EGFL6 Mouse Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 273 amino acids and having a molecular mass of 31.1kDa .
EGFL6 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

EGFL6 protein solution contains  Phosphate Buffered Saline containing 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

ADLTMKKKVK LKMVTPRPAS TRVPKVNLPY SSEEGVSRGR NYDGEQKKKE EGKRERLEEE
KGEKTLRNEV EQERTLRGDV FSPKVNEAED LDLVYVQRKE LNSKLKHKDL NISVDCSFDL
GVCDWKQDRE DDFDWHPADR DNDVGYYMAV PALAGHKKNI GRLKLLLPNL TPQSNFCLLF
DYRLAGDKVG KLRVFVKNSN NALAWEETKN EDGRWRTGKI QLYQGIDTTK SVIFEAERGK GKTGEIAVDG VLLVSGLCPD DFLSVEGHHH HHH.

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

  • EGFL6 Human

ProSpec-HB-EGF Human, His

  • Description
  • HB-EGF Human, His

  • Proheparin-Binding EGF-like Growth Factor Human Recombinant, His Tag
  • CYT-761

Catalogue number

CYT-761

Synonyms

Proheparin-binding EGF-like growth factor, HBEGF, DTR, DTS, HEGFL, HB-EGF, Heparin-binding EGF-like growth factor, Diphtheria toxin receptor, DT-R, DTSF.

Introduction

HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC , fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind heparin and heparin sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

Description

HB-EGF His Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 109 amino acids and having a molecular mass of 12.1kDa.
HB-EGF His 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

The HB-EGF His solution contains 20mM Tris-HCl buffer , 0.2M NaCl, 2mM DTT 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.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 85% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGSDLQEADL DLLRVTLSSK PQALATPNKE EHGKRKKKGK GLGKKRDPCL RKYKDFCIHG ECKYVKELRA PSCICHPGYH GERCHGLSL.

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-EPGN Human, His

  • Description
  • EPGN Human, His

  • Epigen Human Recombinant, His Tag
  • CYT-794

Catalogue number

CYT-794

Synonyms

EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

Introduction

EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.

Description

EPGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids and having a molecular mass of 12.1kDa.
EPGN 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

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

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 MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K

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.

Related Products

  • EPGN Human

ProSpec-EPGN Human, Sf9

  • Description
  • EPGN Human, Sf9

  • Epigen Human Recombinant, Sf9
  • CYT-1038

Catalogue number

CYT-1038

Synonyms

Epithelial mitogen,  EPG, Epithelial Mitogen Homolog , Epithelial Mitogen Homolog, ALGV3072, PRO9904, Epigen, EPGN.

Introduction

EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.

Description

EPGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 10.8kDa .
EPGN is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

EPGN 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

ADPAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE 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.

Related Products

  • EPGN Human, His
  • EPGN Human

ProSpec-EPO a Human, His

  • Description
  • EPO a Human, His

  • Erythropoietin-alpha Human Recombinant, His Tag
  • CYT-791

Catalogue number

CYT-791

Synonyms

Erythropoietin, EP, INN=Epoetin, EPO a, Erythropoietin-alpha, EPO.

Introduction

EPO a is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. EPO a is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. EPO a also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

Description

EPO a Human Recombinant produced in Baculovirus is a single, glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.5kDa.
EPO a 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

EPO a 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% as determined by -PAGE.

Amino acid sequence

APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

Biological Activity

The ED50 range is ≤0.5ng/ml and measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

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

  • EPO a Human
  • EPO a Fc Human
  • EPO a Human, Sf9
  • EPO a Human, HEK
  • EPO Mouse

ProSpec-EPO a Human, Sf9

  • Description
  • EPO a Human, Sf9

  • Erythropoietin-alpha Human Recombinant, Sf9
  • CYT-934

Catalogue number

CYT-934

Synonyms

Erythropoietin, Epoetin, MVCD2, EP, Erythropoietin-Alpha, EPO-a, EPO-alpha.

Introduction

This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

Description

Erythropoietin-alpha Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.5kDa .
EPO-a 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

EPO a 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

APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is ≤ 0.5 ng/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.

Related Products

  • EPO a Human, His
  • EPO a Human
  • EPO a Fc Human
  • EPO a Human, HEK
  • EPO Mouse

ProSpec-EPO Mouse

  • Description
  • EPO Mouse

  • Erythropoietin Mouse Recombinant
  • CYT-1171

Catalogue number

CYT-1171

Synonyms

Erythropoietin, erythropoietin isoform 1 precursor, Epo.

Introduction

Erythropoietin or EPO is a hormone , part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.

Description

EPO Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa.
EPO is fused to 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

EPO Mouse protein 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 95.0% as determined by -PAGE.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

Amino acid sequence

ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.

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

  • EPO a Fc Human
  • EPO a Human
  • EPO a Human, HEK
  • EPO a Human, His
  • EPO a Human, Sf9
  • EPOR Human
  • EPOR Human, Active
  • EPO Rat

ProSpec-FGF 1 Mouse, His

  • Description
  • FGF 1 Mouse, His

  • Fibroblast Growth Factor-acidic Mouse Recombinant, His Tag
  • CYT-072

Catalogue number

CYT-072

Synonyms

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Introduction

Acidic fibroblast growth factor is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

Description

FGF-1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 18kDa .
FGF-1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless clear solution.

Formulation

FGF-1 protein solution containing 20mM Tris-HCl buffer , 1mM DTT, 30% glycerol and 0.1M NaCl.

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 MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

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.

Related Products

  • FGF 1 Human
  • FGF 1 Mouse
  • FGF 1 Human, Sf9
  • FGF 1 Rat
  • FGF1 Human, 154 a.a.

ProSpec-FGF 18 Human, His

  • Description
  • FGF 18 Human, His

  • Fibroblast Growth Factor-18 Human Recombinant, His Tag
  • CYT-935

Catalogue number

CYT-935

Synonyms

Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.

Introduction

Fibroblast growth factor 18 is a member of the large FGF family which has at least 23 members. FGF18 is a binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.

Description

FGF18 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 22.3kDa.

Source

Escherichia Coli.

Physical Appearance

Filtered White lyophilized powder.

Formulation

FGF18 was filtered and lyophilized in phosphate buffered saline and 5% w/v trehalose.

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. FGF18 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

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.

Amino acid sequence

MKHHHHHHASEENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQPELQK PFKYTTVTKR SRRIRPTHPA.

Purity

Purity as determined by densitometric image analysis is greater than 95%.

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.

Related Products

  • FGF 18 Human
  • FGF 18 Mouse
  • FGF-18 Rat

ProSpec-FGF 19 Human, His

  • Description
  • FGF 19 Human, His

  • Fibroblast Growth Factor-19 Human Recombinant, His Tag
  • CYT-279

Catalogue number

CYT-279

Synonyms

Fibroblast growth factor 19, FGF-19.

Introduction

The FGFs are a family of more than 20 small secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors 1, 2, or 3. A fourth closely related tyrosine kinase receptor was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors : FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

Description

Fibroblast Growth Factor-19 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 206 amino acids and having a molecular mass of 23 kDa. The amino acid sequence of the recombinant human FGF19 is 100% homologous to the amino acid sequence of the human FGF19 without signal sequence and contains his tag at N-terminal. The FGF-19 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Filtered white lyophilized powder.

Formulation

Filtered and lyophilized from 0.5mg/ml in 20mM TRIS, 20mM NaCl, pH 7.5.

Solubility

Add deionized water to a working concentration approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.

Stability

Lyophilized FGF-19 Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-19 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.

Amino acid sequence

MRGSHHHHHH GMASLAFSDA GPHVHYGWGD PIRLRHLYTS GPHGLSSCFL RIRADGVVDC ARGQSAHSLLEIKAVALRTV AIKGVHSVRY LCMGADGKMQ GLLQYSEEDC AFEEEIRPDG YNVYRSEKHR LPVSLSSAKQ RQLYKNRGFL PLSHFLPMLP MVPEEPEDLR GHLESDMFSS PLETDSMDPF GLVTGLEAVR SPSFEK.

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.

Related Products

  • FGF 15 Mouse
  • FGF 19 Human
  • FGF19 Human, HEK

ProSpec-FGF 21 Human, His

  • Description
  • FGF 21 Human, His

  • Fibroblast Growth Factor-21 Human Recombinant, His Tag
  • CYT-281

Catalogue number

CYT-281

Synonyms

Fibroblast growth factor 21, FGF-21.

Introduction

The FGFs are a family of more than 20 small secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors 1, 2, or 3. A fourth closely related tyrosine kinase receptor was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors : FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

Description

Fibroblast Growth Factor -21 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 202 amino acids and having a molecular mass of 21.6 kDa .
The FGF-21 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 clear solution.

Formulation

The FGF-21 His tag protein solution in 20mM Tris-HCl buffer 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 .
Please avoid freeze thaw cycles.

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MHPIPDSSPL LQFGGQVRQR YLYTDDAQQT EAHLEIREDG TVGGAADQSP ESLLQLKALK PGVIQILGVKTSRFLCQRPD GALYGSLHFD PEACSFRELL LEDGYNVYQS EAHGLPLHLP GNKSPHRDPA PRGPARFLPL PGLPPAPPEP PGILAPQPPD VGSSDPLSMV GPSQGRSPSY AS.

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.

Related Products

  • FGF 21 Mouse, His
  • FGF 21 Mouse, Sf9
  • FGF 21 Mouse
  • FGF 21 Rat
  • FGF 21 Bovine
  • FGF 21 Human

ProSpec-FGF 21 Mouse, His

  • Description
  • FGF 21 Mouse, His

  • Fibroblast Growth Factor-21 Mouse Recombinant, His Tag
  • CYT-516

Catalogue number

CYT-516

Synonyms

Fibroblast growth factor 21, FGF-21.

Introduction

The FGFs are a family of more than 20 small secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors 1, 2, or 3. A fourth closely related tyrosine kinase receptor was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors : FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

Description

Fibroblast Growth Factor -21 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 21.2 kDa. The amino acid sequence of the recombinant human FGF21 is 100% homologous to the amino acid sequence of the Mouse FGF21 without signal sequence and contains 10 a.a. His tag at N-terminal.
The FGF-21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Filtered white lyophilized powder.

Formulation

Filtered and lyophilized from 0.5 mg/ml in 20mM TRIS, 20mM NaCl, pH 7.5.

Solubility

It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture. Add DTT and NaCl before freezing to prevent potential aggregation.

Stability

Lyophilized FGF-21 Mouse Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 21 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:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

MKHHHHHHAS AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALKPGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDATSWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY AS.

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.

Related Products

  • FGF 21 Mouse, Sf9
  • FGF 21 Human
  • FGF 21 Bovine
  • FGF 21 Mouse
  • FGF 21 Rat
  • FGF 21 Human, His

ProSpec-FGF 21 Mouse, Sf9

  • Description
  • FGF 21 Mouse, Sf9

  • Fibroblast Growth Factor-21 Mouse Recombinant, Sf9
  • CYT-930

Catalogue number

CYT-930

Synonyms

Fibroblast growth factor 21, FGF-21.

Introduction

The FGFs are a family of more than 20 small secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors 1, 2, or 3. A fourth closely related tyrosine kinase receptor was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors : FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

Description

FGF-21 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids and having a molecular mass of 21.0kDa .

FGF21 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered colorless clear solution.

Formulation

FGF-21 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

AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDAT SWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY ASLEHHHHHH.

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.

Related Products

  • FGF 21 Human
  • FGF 21 Rat
  • FGF 21 Bovine
  • FGF 21 Human, His
  • FGF 21 Mouse, His
  • FGF 21 Mouse

ProSpec-FGF 23 Human, His

  • Description
  • FGF 23 Human, His

  • Fibroblast Growth Factor-23 Human Recombinant, His Tag
  • CYT-374

Catalogue number

CYT-374

Synonyms

Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

Introduction

FGF-23 is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. This gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets , an inherited phosphate wasting disorder. Abnormally high level expression of FGF23 was found in oncogenic hypophosphatemic osteomalacia , a phenotypically similar disease caused by abnormal phosphate metabolism. Mutations FGF23 have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.

Description

Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain expressed with a -6xHis tag containing a total of 257 amino acids and having a molecular mass of 28629.5 Dalton.
The FGF-23 is and purified by chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered white lyophilized powder.

Formulation

The protein was lyophilized from 25mM Tris pH7.5 and 0.6M NaCl solution.

Solubility

It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-23 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Fibroblast Growth Factor 23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
FAKFIHHHHHH.

Biological Activity

Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

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

  • FGF23 Human
  • FGF 23 C-term Human

ProSpec-FGF12 Human, His

  • Description
  • FGF12 Human, His

  • Recombinant Human Fibroblast Growth Factor 12, His Tag
  • CYT-620

Catalogue number

CYT-620

Synonyms

FGF-12, FGF12, FGF12B, FHF1, Fibroblast growth factor 12, Fibroblast growth factor homologous factor 1, FHF-1, Myocyte-activating factor.

Introduction

FGF12 is part of the Fibroblast Growth Factor family which has a vast mitogenic and cell survival functions, and play a role in a range of biological activities, among them are embryonic development, cell growth, morphogenesis, tissue repair, tumor growth, and invasion. FGF-12 doesn’t obtain the N-terminal signal sequence present in the majority of the FGF family members, but it contains clusters of basic residues that act as a nuclear localization signal. When transfected into mammalian cells, FGF12 accumulated in the nucleus, but was not secreted. FGF12 is involved in nervous system development and function. FGF12 binds to IB2 , a cellular kinase scaffold, and voltage gated sodium channels and is also involved in intracellular signaling and ion exchange.

Description

The FGF-12 Human recombinant protein is a single, non-glycosylated polypeptide chain produced in E. coli, having a molecular weight of 22.6kDa and containing 201 amino acids . The FGF12 is fused to a 20 amino acid His tag at the N-terminus.

Source

Escherichia Coli.

Physical Appearance

Sterile liquid colorless solution.

Formulation

The FGF-12 solution contains 20mM Tris pH-7.5, 1mM DTT, 2mM EDTA and 10% glycerol.

Stability

Store FGF12 at -20°C. Can be stored at 4°C for a limited period of time of 7 days.

Purity

Greater than 90% as determined by -PAGE.

Amino acid sequence

MSSHHHHHH SSGLVPRGSH MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE YLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR RKSSGTPTM NGGKVVNQDS T.

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

  • FGF12 Human
  • FGF12 Human

ProSpec-FGF17 Human, His

  • Description
  • FGF17 Human, His

  • Fibroblast Growth Factor 17 Human Recombinant, His Tag
  • CYT-755

Catalogue number

CYT-755

Synonyms

Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

Introduction

Fibroblast Growth Factor 17 belongs to the fibroblast growth factor family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a role in central nervous system, bone and vascular development.

Description

FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids and having a molecular mass of 25.2kDa.
FGF17 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

FGF17 protein solution contains 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 90% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGSHMTQGEN HPSPNFNQYV RDQGAMTDQL SRRQIREYQL YSRTSGKHVQ VTGRRISATA EDGNKFAKLI VETDTFGSRV RIKGAESEKY ICMNKRGKLI GKPSGKSKDC VFTEIVLENN YTAFQNARHE GWFMAFTRQG RPRQASRSRQ NQREAHFIKR LYQGQLPFPN HAEKQKQFEF VGSAPTRRTK RTRRPQPLT.

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

  • FGF17 Human
  • FGF17 Mouse

ProSpec-FGF20 Human

  • Description
  • FGF20 Human

  • Fibroblast Growth Factor-20 Human Recombinant
  • CYT-875

Catalogue number

CYT-875

Synonyms

Fibroblast Growth Factor 20, FGF-20, RHDA2, FGF20.

Introduction

Fibroblast growth factor 20 belongs to the FGF gene family and member of FGF-9 subfamily . Human FGF20 has several receptors which include FGF R1c, FGF R2c, FGF R3b, FGF R3c and FGF R4. FGF20 is expressed a various cells, including dopaminergic neurons, fibroblasts, keratinocytes and breast epithelium, and numerous sites in the fetus.

Description

FGF20 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids and having a molecular mass of 24kDa.
The FGF-20 is fused to a 6 amino acid His tag [HHHHHH] at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a 0.2µm filtered solution in MOPS, 2SO4, DTT and EDTA.

Solubility

It is recommended to reconstitute the lyophilized FGF-20 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized FGF20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-20 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 -PAGE.

Amino acid sequence

MHHHHHHAPL AEVGGFLGGL EGLGQQVGSH FLLPPAGERP PLLGERRSAA ERSARGGPGA AQLAHLHGIL RRRQLYCRTG FHLQILPDGS VQGTRQDHSL FGILEFISVA VGLVSIRGVD SGLYLGMNDK GELYGSEKLT SECIFREQFE ENWYNTYSSN IYKHGDTGRR YFVALNKDGT PRDGARSKRH QKFTHFLPRP VDPERVPELY KDLLMYT.

Biological Activity

The ED50, as measured in a proliferation assay using mouse NR6R-3T3 cells, is less than 2.5ng/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.

ProSpec-FGF23 Human, Sf9

  • Description
  • FGF23 Human, Sf9

  • Fibroblast Growth Factor-23 Human Recombinant, Sf9
  • CYT-1102

Catalogue number

CYT-1102

Synonyms

Fibroblast growth factor 23, FGF-23, Phosphatonin, Tumor-derived hypophosphatemia-inducing factor, HYPF.

Introduction

FGF-23 is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, tissue repair, morphogenesis, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. This gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets , an inherited phosphate wasting disorder. a high level expression of FGF23 was found in oncogenic hypophosphatemic osteomalacia , a phenotypically similar disease caused by abnormal phosphate metabolism.

Description

FGF23 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 236 amino acids and having a molecular mass of 26.4kDa .
FGF23 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

FGF23 protein solution containsPhosphate Buffered Saline , 2mM DTT, 1mM EDTA 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

ADPYPNASPL LGSSWGGLIH LYTATARNSY HLQIHKNGHV DGAPHQTIYS ALMIRSEDAG
FVVITGVMSR RYLCMDFRGN IFGSHYFDPE NCRFQHQTLE NGYDVYHSPQ YHFLVSLGRA
KRAFLPGMNP PPYSQFLSRR NEIPLIHFNT PIPRRHTRSA EDDSERDPLN VLKPRARMTP
APASCSQELP SAEDNSPMAS DPLGVVRGGR VNTHAGGTGP EGCRPFAKFI HHHHHH.

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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  • FGF 23 C-term Human
  • FGF 23 Human, His
  • FGF23 Human

ProSpec-IFNAR1 Human

  • Description
  • IFNAR1 Human

  • Interferon Alpha and Beta Receptor Subunit 1 Human Recombinant
  • CYT-1138

Catalogue number

CYT-1138

Synonyms

IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.

Introduction

Interferon Alpha And Beta Receptor or IFNAR1, is part of the class II cytokine receptor family. IFNAR1 forms one of the two chains of a receptor for interferons alpha and beta. IFNAR1 binds and activates the receptor that stimulates Janus protein kinases, which then phosphorylate few proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also acts as an antiviral factor.

Description

IFNAR1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 415 amino acids and having a molecular mass of 47.9kDa. IFNAR1 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

IFNAR1 protein solution contains Phosphate Buffered Saline 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.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH 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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  • IFNAR1 Mouse

ProSpec-LGALS13 Human

  • Description
  • LGALS13 Human

  • Galectin-13 Human Recombinant
  • CYT-004

Catalogue number

CYT-004

Synonyms

Galactoside-binding soluble lectin 13, Galectin-13, Gal-13, Placental tissue protein 13, PP13, Placental protein 13, LGALS13, PLAC8, GAL13.

Introduction

Recombinant Galectin-13 is an E. coli expressed peptide, this protein is one of human placenta specific galectins, like all galectin family, it contains a carbohydrate recognition domain as well. Increased blood concentration was found highly asscoaited with preeclampsia and HELLP syndrome in pregnant women. The molecular weight of galectin-13 is 16kDa.

Description

Recombinant Human LGALS13 produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 16kDa. The LGALS13 also might appear as a homodimer, having a total Mw of 32kDa. LGALS13 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

LGALS13 protein solution is formulated in 1xPBS buffer pH 7.4.

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

MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDM                   DEDSDIAFRFRVHFGNHVVMNRREFGIWMLEETTDYVPFEDGK

QFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSFVKMVQVSRDISLTSVCVCN

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-LGALS14 Human

  • Description
  • LGALS14 Human

  • Galectin-14 Human Recombinant
  • CYT-003

Catalogue number

CYT-003

Synonyms

Placental protein 13-like, Charcot-Leyden crystal protein 2, CLC2, Galectin-14, Gal-14, LGALS14, PPL13, MGC22235.

Introduction

Galectin14, aka LGALS14, is a member of the galectin family of carbohydrate binding proteins. Galectin family members contain one or two carbohydrate recognition domains, which can bind beta-galactoside. The LGALS14 gene is predominantly expressed in the placenta. LGALS14 is expressed intracellularly in the placenta and eosinophils and is released by eosinophils following allergen stimulation. LGALS14 may be involved in the development of allergic inflammation.

Description

LGALS14 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 162 amino acids and having a molecular mass of 18.5kDa. The LGALS14 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

The LGALS14 solution contains 20mM Tris-HCl buffer , 20% glycerol, 0.1M NaCl and 1mM DTT.

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 MGSMSSLPVP YTLPVSLPVG SCVIITGTPI LTFVKDPQLE VNFYTGMDED SDIAFQFRLH FGHPAIMNSR VFGIWRYEEK CYYLPFEDGK PFELCIYVRH KEYKVMVNGQ RIYNFAHRFP PASVKMLQVL RDISLTRVLI SD.

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-LGALS16 Human

  • Description
  • LGALS16 Human

  • Galectin-16 Human Recombinant
  • CYT-993

Catalogue number

CYT-993

Synonyms

Lectin Galactoside Binding Soluble 16, Galectin16, Galectin-16, LGALS-16, LGALS16.

Introduction

Galectin-16 binds lactose with high affinity. LGALS16 is a strong inducer of T-cell apoptosis.

Description

LGALS16 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing having a molecular mass of 16kDa.
The LGALS16 also appears as a homodimer and therefore a 32kDa band is observed as well. LGALS16 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

1x PBS and 25mM arginine.

Stability

The Recombinant LGALS16 protein although stable at 4°C for 1 week, should be stored 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.

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-LGALS2 Human

  • Description
  • LGALS2 Human

  • Galectin-2 Human Recombinant
  • CYT-725

Catalogue number

CYT-725

Synonyms

HL14, Gal-2, Beta-galactoside-binding lectin L-14-II, Lactose-binding lectin 2, S-Lac lectin 2.

Introduction

LGALS2 is a soluble beta-galactoside binding lectin that controls cell-to-cell adhesion and cell-to-extracellular matrix interactions and takes part in tumor progression, pre-mRNA splicing and apoptosis. LGALS2 induces apoptosis in activated T cells and binds to the cytokine lymphotoxin-alpha with threat of myocardial infarction.

Description

LGALS2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 16.8 kDa. The LGALS2 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 Galectin-2 His tag 0.5mg/ml protein solution contains 20mM Tris-HCl pH-8, 0.2M NaCl, 10% glycerol & 1mM DTT.

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

MGSSHHHHHH SSGLVPRGSH MTGELEVKNM DMKPGSTLKI TGSIADGTDG FVINLGQGTD KLNLHFNPRF SESTIVCNSL DGSNWGQEQR
EDHLCFSPGS EVKFTVTFES DKFKVKLPDG HELTFPNRLG HSHLSYLSVR GGFNMSSFKL KE.

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

  • LGALS2 Mouse

ProSpec-LGALS3 Human, His

  • Description
  • LGALS3 Human, His

  • Galectin-3 Human Recombinant, His Tag
  • CYT-693

Catalogue number

CYT-693

Synonyms

Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.

Introduction

Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.

Description

LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 270 amino acids and having a molecular mass of 28.3 kDa. The LGALS3 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 Galectin-3 protein solution contains 20mM Tris-HCl buffer , 0.1M NaCl, 1mM DTT 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

The ED50 for this effect is < 2.5ug/ml as measured by its ability to agglutinate human red blood cells.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.

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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  • LGALS3 Human
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ProSpec-LGALS7 Human, His

  • Description
  • LGALS7 Human, His

  • Galectin-7 Human Recombinant, His Tag
  • CYT-617

Catalogue number

CYT-617

Synonyms

Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.

Introduction

Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD . Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.

Description

Galectin-7 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a molecular mass of 17.2kDa.
The Galectin-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

The Galectin-7 solution 20mM Tris-HCl buffer , 10% glycerol and 1mM DTT.

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

MGSSHHHHHH SSGLVPRGSH MSNVPHKSSL PEGIRPGTVL RIRGLVPPNA SRFHVNLLCG EEQGSDAALH FNPRLDTSEV VFNSKEQGSW GREERGPGVP FQRGQPFEVL IIASDDGFKA VVGDAQYHHF RHRLPLARVR LVEVGGDVQL DSVRIF.

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

  • LGALS7 Mouse
  • LGALS7 Human

ProSpec-LGALS8 Human, His

  • Description
  • LGALS8 Human, His

  • Galectin-8 Human Recombinant, His Tag
  • CYT-727

Catalogue number

CYT-727

Synonyms

Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.

Introduction

LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.

Description

LGALS8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids and having a molecular mass of 37.9 kDa. The LGALS8 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 Galectin-8 His tag 0.5mg/ml protein solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, 10% glycerol & 1mM DTT.

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

MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.

Purity

Greater than 90.0% as determined by -PAGE.

Biological Activity

The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/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.

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ProSpec-GDF11 Human, His/CYT-887,Growth and Differentiation factor 11 Human Recombinant, His Tag

ProSpec GDF11 Human His,ProSpec CYT-887,Growth and Differentiation factor 11 Human Recombinant, His Tag,GDF-11 属于骨形态发生蛋白家族和 TGF-β 超家族。 GDF-11 是控制肌肉和神经发育的中枢发育因子。 在成人中,GDF-11 通过心肌细胞的恢复促进心脏肥大逆转。

GDF11 Human, His

Growth and Differentiation factor 11 Human Recombinant, His Tag
CYT-887
ProSpec-GDF11 Human, His/CYT-887 5µg
ProSpec-GDF11 Human, His/CYT-887 20µg
ProSpec-GDF11 Human, His/CYT-887 1mg

Catalogue number

CYT-887

Synonyms

Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
生长分化因子 11、BMP11、骨形态发生蛋白 11、BMP-11、GDF-11、生长/分化因子 11、生长/分化因子 11。

Introduction

GDF-11 belongs to the bone morphogenetic protein family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
GDF-11 属于骨形态发生蛋白家族和 TGF-β 超家族。 GDF-11 是控制肌肉和神经发育的中枢发育因子。 在成人中,GDF-11 通过心肌细胞的恢复促进心脏肥大逆转。

Description

GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 14.8kDa.

GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

在大肠杆菌中产生的 GDF11 Human Recombinant 是单条非糖基化多肽链,包含 132 个氨基酸,分子量为 14.8kDa。

GDF11 在 N 末端与 23 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 colorless solution.

Formulation

GDF11 protein solution containing 20mM Tris-HCl 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 85.0% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.

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 的产品仅供实验室研究使用。 该产品不得用作药物、农业或农药产品、食品添加剂或家用化学品。

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ProSpec-GHBP Human, His

  • Description
  • GHBP Human, His

  • Growth Hormone Binding Protein Human Recombinant, His Tag
  • CYT-921

Catalogue number

CYT-921

Synonyms

Growth Hormone Receptor, Growth Hormone Binding Protein, Somatotropin Receptor GH Receptor, Serum Binding Protein, GHBP, GHIP.

Introduction

Growth hormone receptor, also known as GHR is part of the cytokine receptor family.  GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, growth hormone performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.

Description

GHBP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 254 amino acids and having a molecular mass of 29.4kDa.
GHBP 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

GHBP 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

The ED50 range ≤ 10ng/ml and is measured by ability to inhibit GH-induced proliferation assay using Nb2-11 Rat lymphoma cells in the presence of 1.25ng/ml of human growth hormone.

Amino acid sequence

FSGSEATAAI LSRAPWSLQS VNPGLKTNSS KEPKFTKCRS PERETFSCHW TDEVHHGTKN LGPIQLFYTR RNTQEWTQEW KECPDYVSAG ENSCYFNSSF TSIWIPYCIK LTSNGGTVDE KCFSVDEIVQ PDPPIALNWT LLNVSLTGIH ADIQVRWEAP RNADIQKGWM VLEYELQYKE
VNETKWKMMD PILTTSVPVY SLKVDKEYEV RVRSKQRNSG NYGEFSEVLY VTLPQMSQFT CEEDFYLEHH HHHH.

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-GHBP Human, Sf9

  • Description
  • GHBP Human, Sf9

  • Growth Hormone Binding Protein Human Recombinant, Sf9
  • CYT-1152

Catalogue number

CYT-1152

Synonyms

GHR, GHBP, GHIP.

Introduction

Growth Hormone Binding Protein or GHR, is a protein, part of the cytokine receptor superfamily. GHR binds to 2 receptors, therefore it enhances signal transduction via dimerization of receptors. In elevated levels, growth hormone operates as an antagonist due to high variance in the binding sites affinities. The antagonist operation can be embellished even more when the binding site is reduced its affinity.

Description

GHBP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids and having a molecular mass of 29.4kDa.
GHBP is fused to a 8 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 GHBP 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 95.0% as determined by -PAGE.

Biological Activity

Measured by ability to inhibit GH-induced proliferation assay using Nb2-11 Rat lymphoma cells in the presence of 1.25ng/ml of human growth hormone. The ED50 for this effect is equal or less than 10ng/ml.

Amino acid sequence

FSGSEATAAI LSRAPWSLQS VNPGLKTNSS KEPKFTKCRS PERETFSCHW TDEVHHGTKN LGPIQLFYTR RNTQEWTQEW KECPDYVSAG ENSCYFNSSF TSIWIPYCIK LTSNGGTVDE KCFSVDEIVQ PDPPIALNWT LLNVSLTGIH ADIQVRWEAP RNADIQKGWM VLEYELQYKE VNETKWKMMD PILTTSVPVY SLKVDKEYEV RVRSKQRNSG NYGEFSEVLY VTLPQMSQFT
CEEDFYLEHH 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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ProSpec-GHBP Rat

  • Description
  • GHBP Rat

  • GH Binding Protein Rat Recombinant
  • CYT-933

Catalogue number

CYT-933

Synonyms

GHBP, GH receptor.

Introduction

GH receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, GH performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.

Description

GHBP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 255 amino acids and having a molecular mass of 29.4kDa .
GHBP is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

GHBP 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

FPGSGATPAT LGKASPVLQR INPSLRESSS GKPRFTKCRS PELETFSCYW TEGDDHNLKV PGSIQLYYAR RIAHEWTPEW KECPDYVSAG ANSCYFNSSY TSIWIPYCIK LTTNGDLLKE KCFTVDEIVQ PDPPIGLNWT LLNISLPGIR GDIQVSWQPP PSADVLKGWI ILEYEIQYKE VNETKWKTMS PIWSTSVPLY SLRLDKEHEV RVRSRQRSFE KYSEFSEVLR VTFPQMDTLA ACEEDFRLEH HHHHH.

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-IGFBP 4 Human

  • Description
  • IGFBP 4 Human

  • Insulin-Like Growth Factor Binding Protein-4 Human
  • CYT-030

Catalogue number

CYT-030

Synonyms

Insulin-like growth factor-binding protein 4, IBP-4, IGF-binding protein 4, IGFBP-4, IGFBP4, IBP4, BP-4, HT29-IGFBP.

Introduction

Insulin-like growth factor-binding protein 4 belongs to the insulin-like growth factor binding protein family. IGFBP4 includes an IGFBP domain and a thyroglobulin type-I domain. IGFBP4 binds both insulin-like growth factors I and II. IGFBP-4 circulates in the plasma in both glycosylated and non-glycosylated forms. IGFBPs can either inhibit or enhance the biological activities of IGF, or act in an IGF independent manner. IGFBP-4 is exceptional since it consistently inhibits several cancer cells in vivo and in vitro, suggesting that it may function as an apoptotic factor. IGFBP4 is produced by all colon cancer cells. Binding of IGFBP-4 prolongs the half-life of the IGFs and changes their interaction with cell surface receptors.

Description

IGFBP-4 Human Recombinant amino acids Asp22- Glu258, produced in HEK293 cells and fused with a polyhistidine tag at the C-terminus. IGFBP4 predicted Mw is 27kDa and on -PAGE appears as a 32kDa band under denaturing conditions.
IGFBP4 is purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

IGFBP 4 was lyophilized after extensive dialysis against PBS.

Solubility

It is recommended to reconstitute the lyophilized IGFBP4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized IGFBP4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP-4 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.

Amino acid sequence

DEAIHCPPCS EEKLARCRPP VGCEELVREP GCGCCATCAL GLGMPCGVYT PRCGSGLRCY PPRGVEKPLH TLMHGQGVCM ELAEIEAIQE SLQPSDKDEG DHPNNSFSPC SAHDRRCLQK HFAKIRDRST SGGKMKVNGA PREDARPVPQ GSCQSELHRA LERLAASQSR THEDLYIIPI PNCDRNGNFH PKQCHPALDG QRGKCWCVDR KTGVKLPGGL EPKGELDCHQ LADSFRE + His Tag.

Biological Activity

The ED50 range is 0.01-0.09µg/ml as measured by its ability to inhibit the biological activity of IGFII on MCF7 human breast adenocarcinoma 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-IGFBP3 Human, His

  • Description
  • IGFBP3 Human, His

  • Insulin Like Growth Factor Binding Protein-3 Human Recombinant, His Tag
  • CYT-879

Catalogue number

CYT-879

Synonyms

Insulin-like growth factor-binding protein 3, Insulin Like Growth Factor Binding Protein-3, His Tag, IGFBP3, IBP-3, IGF-binding protein 3, IGFBP-3, IBP3, BP-53, Insulin-like growth factor binding protein 3 isoform b precursor.

Introduction

IGFBP3 is a member of the insulin-like growth factor binding protein family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit and either insulin-like growth factor I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

Description

IGFBP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids and having a molecular mass of 31kDa.
IGFBP3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

IGFBP3 protein solution containing 20mM Tris-HCl buffer 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 analysis by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGASSAGLGP VVRCEPCDAR ALAQCAPPPA VCAELVREPG CGCCLTCALS EGQPCGIYTE RCGSGLRCQP SPDEARPLQA LLDGRGLCVN ASAVSRLRAY LLPAPPAPGN ASESEEDRSA GSVESPSVSS THRVSDPKFH PLHSKIIIIK KGHAKDSQRY KVDYESQSTD TQNFSSESKR ETEYGPCRRE MEDTLNHLKF LNVLSPRGVH IPNCDKKGFY KKKQCRPSKG RKRGFCWCVD KYGQPLPGYT TKGKEDVHCY SMQSK.

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-IGFBP6 Human

  • Description
  • IGFBP6 Human

  • IGFBP-6 Human Recombinant
  • CYT-258

Catalogue number

CYT-258

Synonyms

IGFBP-6, IBP-6, IGF-binding protein 6.

Introduction

IGFBP6 plays a role in lipoprotein assembly and dietary cholesterol absorption. in addition to its acyltransferase activity, it may act as a ligase. may provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.

Description

IGFBP6 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 148-240 and having a molecular mass of 20 kDa including 4kDa His tag.
IGFBP6 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

IBP-6 was lyophilized from a concentrated solution containing 1xPBS, 0.1% and 1mM DTT.

Solubility

It is recommended to reconstitute the lyophilized IGFBP6 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized IBP6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP-6 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 80.0% 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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