IrvineScientific HEK293细胞培养基

产品简介:

BalanCD HEK293 是一个可扩展的系统,旨在支持 HEK293 细胞系在悬浮培养中的生长和转染。这个高度通用的系统由 BalanCD HEK293 培养基、BalanCD HEK293 饲料和抗结块补充剂组成,支持一系列应用,包括生产用于基因治疗的病毒载体、瞬时蛋白表达和重组蛋白生产。 BalanCD HEK293 是可扩展的 BalanCD 培养基和补充剂平台的一部分,旨在提供生长和生产之间的最佳平衡,以最大限度地提高哺乳动物细胞培养的生产力。

产品名称:IrvineScientific HEK293细胞培养基

产品货号:91165

 

产品特点:

• 快速、可扩展地生产病毒载体

• 对多种 HEK293 细胞系使用相同的系统

• 提高瞬时蛋白质表达的生产力 满足监管要求

• 化学成分明确,不含动物成分

• 药物主文件 (DMF) 提交美国食品和药物管理局

 

产品优势:

1.使用相同的生长培养基进行播种、转染和生产

2.可扩展的方案,用于烧瓶、转瓶和生物反应器

3.添加互补的 BalanCD HEK293 补料和/或抗结块添加剂,以最大限度地提高生长和滴度

 

 

产品使用预期:

EK293VC 细胞在 2 L 工作体积的生物反应器中培养。 PEI 介导的 3 种质粒转染在接种后 3 天进行,DNA:PEI 比率为 1:1.5。测定细胞直径。在转染后 48、72 和 96 小时测量 AAV 滴度。

 

 

储存与运输:

本产品在 2-8°C 温度下以冷包装运输。效期1年。

 

产品订购信息

品牌                 货号                 名称                  规格

IrvineScientific 91154  PRIME-XV T Cell CDM     1L

 

产品名称:IrvineScientific HEK293细胞培养基

产品货号:91165

 

关于公司:

Irvine Scientific是JX Holdings集团成员,是细胞培养基和试剂设计、制造和分销的*者,这些培养基和试剂用于工业细胞培养、细胞疗法、细胞遗传学和辅助生育技术(ART)领域。Irvine Scientific是全球培养基提供商,接受监管并同时符合ISO和FDA规范,在美国加州和日本东京两地均有制造设施。

IrvineScientific HEK293成分限定培养基

balanCD HEK293 培养基是一种多功能、化学成分明确、无动物成分的培养基,针对病毒载体和重组蛋白的转染和生产进行了优化。

产品名称:IrvineScientific HEK293成分限定培养基

产品货号:91165

产品特点:

1.满足监管要求

2.化学成分明确,不含动物成分向美国 FDA 提交的药物主文件 (DMF)

产品优势:

1.使用相同的生长培养基进行播种、转染和生产

2.可扩展的方案,用于烧瓶、转瓶和生物反应器

3.添加互补的 BalanCD HEK293 补料和/或抗结块添加剂,以最大限度地提高生长和滴度

产品使用预期:

HEK293T 细胞在 BalanCD HEK293 培养基中的 2 L 工作体积生物反应器中培养,每 3-4 天传代一次。 PEI 介导的 4 个质粒转染在接种后 3 天进行,DNA:PEI 比率为 1:1.5。测定活细胞密度。在转染后 24、48 和 72 小时测量慢病毒滴度。

储存与运输:

本产品在 2-8°C 温度下以冷包装运输。效期1年。

产品应用:

1.快速、可扩展地生产用于基因治疗的病毒载体(腺相关病毒 (AAV)、慢病毒)

2.瞬时蛋白表达和重组蛋白生产至克级产量

 

产品订购信息

品牌                 货号                 名称                  规格

IrvineScientific 91154  PRIME-XV T Cell CDM     1L

产品名称:IrvineScientific HEK293成分限定培养基

产品货号:91165

关于公司:

Irvine Scientific是JX Holdings集团成员,是细胞培养基和试剂设计、制造和分销的*者,这些培养基和试剂用于工业细胞培养、细胞疗法、细胞遗传学和辅助生育技术(ART)领域。Irvine Scientific是全球培养基提供商,接受监管并同时符合ISO和FDA规范,在美国加州和日本东京两地均有制造设施。

Cygnus HEK 293 HCP检测试剂盒

产品名称:Cygnus HEK 293 HCP检测试剂盒

产品货号:   G650S

英文名称:HEK 293 HCP Assay Reagent Set for Gyrolab

产品规格:1 set

产品品牌:Cygnus

 

产品简介:

HEK 293 HCP Assay Reagent Set for Gyrolab®是专为确定在HEK 293细胞系表达的产品中宿主细胞蛋白污染的存在而设计的。该试剂盒应与Gyrolab®Bioaffy™1000 HC检测工具箱一起使用,该试剂盒由gyroprotein Technologies提供。这种方法使用简单,高通量,半定量分析是一种方法,以帮助优化纯化工艺开发,过程控制,常规质量控制和产品批次放行。它来源于与Cygnus第3代hek293 HCP ELISA试剂盒(Cat# F650S)相同的抗体和抗原。这些试剂是“通用的”,因为它们的目的是与几乎所有可能污染产品的宿主细胞蛋白(HCPs)发生反应,而不受纯化过程的影响。该抗体已在山羊和兔子中产生,并使用在无蛋白条件培养基中发现的hek293 HCPs进行抗原亲和纯化。试剂集和Bioaffy 1000 HC分析工具箱的组合优化用于Gyrolab自动化免疫分析系统,可在75分钟内生成96个数据点,无需人工干预。使用Gyrolab Evaluator软件对结果进行评估。

 

产品参数:

产品类型:ELISA试剂盒

储存:标准品-10°C至-30°C,所有其他试剂盒试剂2°C至8°C

目的表达系统:hek293

种群:哺乳动物

反应性:人类

 

产品应用:

本试剂组是用于测定产品中存在宿主细胞蛋白污染在hek293细胞系中表达。

试剂组用于研究和生产,仅用于人类或动物。

 

产品名称:Cygnus HEK 293 HCP检测试剂盒

产品货号:   G650S

关于公司:

Cygnus Technologies是生物制药行业在宿主细胞蛋白(HCP)和其他工艺相关的杂质检测和分析方面的合作伙伴。此外,Cygnus现在还提供创新的病毒清除解决方案。

Cygnus帮助公司开发治疗性蛋白质、疫苗、抗体、血浆衍生物和基因疗法,以确保生物治疗药物在人体试验、监管批准和商业释放前的安全性。Cygnus提供分析工具和解决方案,提供见解,以改善生物工艺开发,以更快的监管批准和更好的临床结果。

ProSpec-G CSF Human

  • Description
  • G CSF Human

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

Catalogue number

CYT-220

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Amino acid sequence

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

Purity

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

Biological Activity

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

Protein content

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

Usage

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

References

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

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ProSpec-G CSF Human, CHO

  • Description
  • G CSF Human, CHO

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

Catalogue number

CYT-329

Synonyms

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

Introduction

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

Description

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

Source

Chinese Hamster Ovary Cells .

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Amino acid sequence

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

Purity

Greater than 97.0% as determined by -PAGE.

Biological Activity

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

Usage

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

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ProSpec-G CSF Human, HEK

  • Description
  • G CSF Human, HEK

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

Catalogue number

CYT-088

Synonyms

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

Introduction

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

Description

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

Source

HEK.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Purity

Greater than 95% as obsereved by -PAGE.

Biological Activity

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

Usage

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

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ProSpec-G CSF Human, His

  • Description
  • G CSF Human, His

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

Catalogue number

CYT-476

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

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

Stability

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

Purity

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

Usage

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

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ProSpec-G CSF Human, PEG

  • Description
  • G CSF Human, PEG

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

Catalogue number

CYT-018

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Colorless, clear and transparent solution.

Formulation

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

Stability

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

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

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

Usage

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

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ProSpec-G CSF Mouse

  • Description
  • G CSF Mouse

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

Catalogue number

CYT-410

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Amino acid sequence

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

Purity

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

Biological Activity

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

Usage

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

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ProSpec-GCSF Monkey

  • Description
  • GCSF Monkey

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

Catalogue number

CYT-1121

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Purity

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

Amino acid sequence

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

Biological Activity

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

Usage

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

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ProSpec-GCSF Rat

  • Description
  • GCSF Rat

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

Catalogue number

CYT-940

Synonyms

Granulocyte colony stimulating factor, Protein Csf3, Csf3.

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Purity

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

Amino acid sequence

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

Biological Activity

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

Usage

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

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ProSpec-M CSF Human

  • Description
  • M CSF Human

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

Catalogue number

CYT-308

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Amino acid sequence

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

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

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

Usage

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

References

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

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

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ProSpec-M CSF Human, Baculovirus

  • Description
  • M CSF Human, Baculovirus

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

Catalogue number

CYT-637

Synonyms

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

Introduction

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

Description

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

Source

Baculovirus infected Silkworm.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Amino acid sequence

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

Purity

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

Biological Activity

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

Usage

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

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ProSpec-M CSF Human, HEK

  • Description
  • M CSF Human, HEK

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

Catalogue number

CYT-106

Synonyms

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

Introduction

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

Description

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

Source

HEK.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Purity

Greater than 95% as obsereved by -PAGE.

Biological Activity

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

Usage

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

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ProSpec-M CSF Human, His

  • Description
  • M CSF Human, His

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

Catalogue number

CYT-695

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile filtered colorless solution.

Formulation

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

Stability

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

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

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

Usage

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

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ProSpec-M CSF Human, Sf9 His

  • Description
  • M CSF Human, Sf9 His

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

Catalogue number

CYT-1015

Synonyms

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

Introduction

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

Description

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

Source

Sf9, Insect cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

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

Stability

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

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

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

Amino acid sequence

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

Usage

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

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ProSpec-M CSF Mouse

  • Description
  • M CSF Mouse

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

Catalogue number

CYT-439

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Amino acid sequence

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

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

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

Usage

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

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ProSpec-M CSF Rat

  • Description
  • M CSF Rat

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

Catalogue number

CYT-856

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

Amino acid sequence

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

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

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

Usage

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

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ProSpec-M CSF Rat HEK

  • Description
  • M CSF Rat HEK

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

Catalogue number

CYT-046

Synonyms

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

Introduction

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

Description

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

Source

HEK293

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The recombinant MCSF was lyophilized after extensive dialysis against PBS.

Solubility

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

Stability

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

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

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

Usage

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

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ProSpec-MCSF Mouse, Sf9

  • Description
  • MCSF Mouse, Sf9

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

Catalogue number

CYT-1141

Synonyms

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

Introduction

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

Description

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

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

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

Stability

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

Purity

Greater than 90.0% as determined by -PAGE.

Biological Activity

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

Amino acid sequence

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

Usage

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

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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.

Related Products

  • CTGF Human, His
  • CTGF Human
  • CTGF Human, HEK
  • CTGF Antibody
  • CTGF Mouse
  • CTGF Human

ProSpec-CTGF Human

  • Description
  • CTGF Human

  • Connective Tissue Growth Factor Human Recombinant
  • CYT-541

Catalogue number

CYT-541

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

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

Solubility

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

Stability

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

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

Please prevent freeze-thaw cycles. 

Purity

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

Biological Activity

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

Amino acid sequence

MGKKCIRTPK ISKPIKFELS GCTSMKTYRA KFCGVCTDGR CCTPHRTTTL PVEFKCPDGE VMKKNMMFIK TCACHYNCPG DNDIFESLYY RKMYGDMA.

Usage

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

Related Products

  • CTGF Human
  • CTGF Human, HEK
  • CTGF Human, His
  • CTGF Antibody
  • CTGF Mouse
  • CTGF Human

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.

Related Products

  • CTGF Human
  • CTGF Human
  • CTGF Human, HEK
  • CTGF Human, His
  • CTGF Antibody
  • CTGF Mouse

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.

Related Products

  • CTGF Human
  • CTGF Human
  • CTGF Human, His
  • CTGF Antibody
  • CTGF Mouse
  • CTGF Human

ProSpec-CTGF Human, His

  • Description
  • CTGF Human, His

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

Catalogue number

CYT-438

Synonyms

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

Introduction

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

Description

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

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

Stability

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

Purity

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

Amino acid sequence

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

Usage

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

Related Products

  • CTGF Human, HEK
  • CTGF Human
  • CTGF Human
  • CTGF Antibody
  • CTGF Mouse
  • CTGF Human

ProSpec-CTGF Mouse

  • Description
  • CTGF Mouse

  • Connective Tissue Growth Factor Mouse Recombinant
  • CYT-1173

Catalogue number

CYT-1173

Synonyms

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

Introduction

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

Description

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

Source

HEK293

Physical Appearance

Filtered clear solution.

Formulation

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

Stability

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

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

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

Usage

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

Related Products

  • CTGF Human
  • CTGF Antibody
  • CTGF Human
  • CTGF Human, HEK
  • CTGF Human, His
  • CTGF Human

ProSpec-EGFL6 Human

  • Description
  • EGFL6 Human

  • EGF Like Domain Multiple 6 Human Recombinant
  • CYT-974

Catalogue number

CYT-974

Synonyms

EGF Like Domain Multiple 6, MAM and EGF Domains-Containing Gene Protein, MAM and EGF Domain Containing, EGF-Like Protein 6, MAEG, EGF Repeat-Containing Protein 6, W80, EGFL6.

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

EGF Like Domain Multiple 6 Human Recombinant produced in HEK cells is a polypeptide chain starting at amino acid Asn at position 22 to amino acid Arg at position 363, fused to an FC, 6 x His-tag at C-terminus, containing a total of 348 amino acids and having a predicted molecular mass of 40-55kDa. The EGFL6 is purified by proprietary chromatographic techniques.

Source

HEK .

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The EGFL6 protein was lyophilized from a 0.2µm filtered solution in 20mM MES and 500mM NaCl, pH 6.0 with 5% Trehalose.

Solubility

It is recommended to reconstitute the lyophilized EGFL6 in sterile PBS at 500µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized EGFL6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGFL6 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.

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.

Biological Activity

EGFL6 activity is determined by its ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The expected ED50 for this effect is 1-5 μg/ml.

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ProSpec-EPO a Fc Human

  • Description
  • EPO a Fc Human

  • Erythropoietin-Alpha Fc-Chimera Human Recombinant
  • CYT-325

Catalogue number

CYT-325

Synonyms

EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

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 Fc-Chimera Human Recombinant is produced in Chinese hamster ovary cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing -PAGE.

Source

Chinese Hamster Ovary Cells.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Each mg of lyophilized powder contains 1x PBS pH-7.4.

Solubility

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

Stability

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

Purity

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

Biological Activity

The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.

Usage

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

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ProSpec-EPO a Human

  • Description
  • EPO a Human

  • Erythropoietin-Alpha Human Recombinant
  • CYT-201

Catalogue number

CYT-201

Synonyms

Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.

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 is produced in Chinese hamster ovary cells by recombinant DNA technology is a single, polypeptide chain containing 166 amino acids and having a predicted molecular mass of 21,000 Dalton and apparent glycosylated molecular mass of 36-40kDa. EPO-a is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Each mg of lyophilized powder contains 0.59 mg sodium citrate, 0.58 mg sodium chloride and 0.006 mg citric acid.

Solubility

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

Stability

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

Purity

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

Amino acid sequence

APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDR.

Biological Activity

The Specific Activity was measured by Normocyth -aemic mice and was found to be 150,000 IU/mg.

References

1.Title:Zinc Transporters ZnT1 , Zip8 , and Zip10 in Mouse Red Blood Cells Are Differentially Regulated during Erythroid Development and by Dietary Zinc Deficiency1–3
Publication:Journal of Nutrition, doi:10.3945/jn.108.093575
Vol. 138, No. 11, 2076-2083, November 2008
© 2008 American Society for Nutrition J. Nutr. 138:2076-2083, November 2008
Link:http://jn.nutrition.org/content/138/11/2076.full

2.Title:Systemically delivered Erythropoietin transiently enhances adult hippocampal neurogenesis.
Publication:Article first published online: 7 MAY 2007 DOI:10.1111/j.1471-4159.2007.04684.x Journal of Neurochemistry  Volume 102, Issue 6, pages 1953–1965, September 2007.
Link:http://onlinelibrary.wiley.com/doi/10.1111/j.1471-4159.2007.04684.x/full

3.Title:ZINC TRANSPORTER EXPRESSION IN MATURE RED BLOOD CELLS AND
DIFFERENTIATING ERYTHROID PROGENITOR CELLS.
Publication:UNIVERSITY OF FLORIDA
© 2007 Moon-Suhn Ryu
Link:http://ufdcimages.uflib.ufl.edu/UF/E0/02/14/46/00001/ryu_m.pdf

4.Title:Cell Therapy with Human Renal Cell Cultures Containing Erythropoietin-Positive Cells Improves Chronic Kidney Injury.
Publication:First Published Online May 3, 2012 doi: 10.5966/sctm.2011-0048 Stem Cells Trans Med May 2012 vol. 1 no. 5 373-383
Link:http://stemcellstm.alphamedpress.org/content/1/5/373.full

Usage

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

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ProSpec-EPO a Human, HEK

  • Description
  • EPO a Human, HEK

  • Erythropoietin-alpha Human Recombinant, HEK
  • CYT-083

Catalogue number

CYT-083

Synonyms

Erythropoietin-Alpha, EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

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

EPO-a Human Recombinant produced in HEK cells is a glycosylated monomer, having a total molecular weight of 36kDa.
The EPO-alpha is purified by proprietary chromatographic techniques.

Source

HEK.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The EPO-alpha was lyophilized from 1mg/ml in 1xPBS.

Solubility

It is recommended to reconstitute the lyophilized EPO-alpha in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

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

Purity

Greater than 95% as obsereved by -PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells and is typically 0.5-2.5ng/ml, corresponding to a specific activity of 400,000-2,000,000 units/mg.

Usage

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

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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.

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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.

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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.

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  • EPO Rat

ProSpec-EPO Rat

  • Description
  • EPO Rat

  • Erythropoietin Rat Recombinant
  • CYT-1187

Catalogue number

CYT-1187

Synonyms

Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142. 

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 Rat Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19.6 kDa. EPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

EPO protein 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 TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

Amino acid sequence

DGSAPPRLIC DSRVLERYIL EAKEAENVTM GCAEGPRLSE NITVPDTKVN FYAWKRMKVE EQAVEVWQGL SLLSEAILQA QALQANSSQP PESLQLHIDK AISGLRSLTS LLRVLGAQKE LMSPPDATQA APLRTLTADT FCKLFRVYSN FLRGKLKLYT GEACRRGDRH HHHHH.

Usage

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

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ProSpec-FGF 19 Human

  • Description
  • FGF 19 Human

  • Fibroblast Growth Factor-19 Human Recombinant
  • CYT-700

Catalogue number

CYT-700

Synonyms

Fibroblast growth factor 19, FGF-19, FGF19.

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 INS desensitization and to improve INS, 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

FGF19 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.8 kDa.
The FGF-19 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Filtered white lyophilized powder.

Formulation

Filtered and lyophilized from 1mg/ml in 1xPBS, pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized FGF-19 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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.

Biological Activity

The ED50 as determined by the dose-dependent stimulation of the proliferation of balb/c 3T3 cells is 100-150ng/ml.

Purity

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

Amino acid sequence

MRPLAFSDAG PHVHYGWGDP IRLRHLYTSG PHGLSSCFLR IRADGVVDCA RGQSAHSLLE IKAVALRTVA IKGVHSVRYL CMGADGKMQG LLQYSEEDCA FEEEIRPDGY NVYRSEKHRL PVSLSSAKQR QLYKNRGFLP LSHFLPMLPM VPEEPEDLRG HLESDMFSSP LETDSMDPFG LVTGLEAVRS PSFEK.

Usage

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

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ProSpec-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.

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ProSpec-FGF 8 Human

  • Description
  • FGF 8 Human

  • Fibroblast Growth Factor-8 Human Recombinant
  • CYT-839

Catalogue number

CYT-839

Synonyms

FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

Introduction

FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.

Description

FGF 8 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa. 

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a sterile 0.2 micron filtered aqueous solution containing 0.1% TFA.

Solubility

It is recommended to reconstitute the lyophilized FGF-8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized FGF-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-8 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 -PAGE.

Amino acid sequence

MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGD

PFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR.

Biological Activity

The ED50, as determined by its ability to induce proliferation of NR6-R 3T3, is 0.915ng/ml, corresponding to a specific activity of 1.1×106units/mg.

Usage

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

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ProSpec-FGF 8 Mouse

  • Description
  • FGF 8 Mouse

  • Fibroblast Growth Factor-8 Mouse Recombinant
  • CYT-070

Catalogue number

CYT-070

Synonyms

Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.

Introduction

FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.

Description

FGF-8 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids and having a molecular mass of 28.1kDa.
The FGF-8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

FGF-8 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized FGF-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized FGF-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-8 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

QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR.

Biological Activity

The ED50, as determined by the dose-dependent a cell proliferation assay using NR6R-3T3 mouse fibroblast cells is <25 ng/ml in the presence of 0.1 ug/ml heprin, corresponding to a specific activity of > 4.0×104 units/mg.

Usage

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

Related Products

  • FGF8 Human, HEK
  • FGF 8 Mouse, 194 a.a.
  • FGF 8 Human

ProSpec-FGF 8 Mouse, 194 a.a.

  • Description
  • FGF 8 Mouse, 194 a.a.

  • Fibroblast Growth Factor-8 Mouse Recombinant, 194 a.a.
  • CYT-840

Catalogue number

CYT-840

Synonyms

FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

Introduction

FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.

Description

FGF 8 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa. 

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a concentrated solution containing 5mM Na3PO4 and 50 mM NaCl, pH 7.5.

Solubility

It is recommended to reconstitute the lyophilized FGF 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. 

Stability

Lyophilized FGF 8 although stable at room temperature for 3 weeks, should be stored desiccated below -18?C. Upon reconstitution FGF 8 should be stored at 4?C between 2-7 days and for future use below -18?C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

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

Amino acid sequence

MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGD
PFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR

Biological Activity

The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

Usage

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

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  • FGF 8 Human
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ProSpec-FGF19 Human, HEK

  • Description
  • FGF19 Human, HEK

  • Fibroblast Growth Factor-19 Human Recombinant, HEK
  • CYT-1180

Catalogue number

CYT-1180

Synonyms

fibroblast growth factor 19, FGF19.

Introduction

Fibroblast Growth Factor-19 is a member of the FGF family. FGF-19 interacts with FGFR1, FGFR2, FGFR3 and FGFR4. T FGF-19 takes part in the suppression of bile acid biosynthesis through downregulation of CYP7A1 expression, following positive regulation of the JNK and EPK1/2 cascades. FGF-19 stimulates glucose uptake in adiposytes and is a high affinity, heparin dependent ligand for FGFR4.

Description

FGF19 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 205 amino acids and having a molecular mass of 23.0 kDa.
FGF19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

FGF19 protein contains 20mM Tris-HCl, 20% 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 95.0% as determined by -PAGE. 

Amino acid sequence

DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH 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.

Related Products

  • FGF 19 Human
  • FGF 19 Human, His

ProSpec-FGF8 Human, HEK

  • Description
  • FGF8 Human, HEK

  • Fibroblast Growth Factor-8 Human Recombinant, HEK
  • CYT-087

Catalogue number

CYT-087

Synonyms

FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

Introduction

FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.

Description

FGF-8 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 30-45kDa due to glycosylation.
The FGF8 is purified by proprietary chromatographic techniques.

Source

HEK.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The FGF-8 was lyophilized in 10mM Tris-HCl pH 7.4 and 800mM NaCl.

Solubility

It is recommended to reconstitute the lyophilized FGF8 in sterile water containing 0.1% endotoxin-free recombinant HSA.

Stability

Lyophilized FGF-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF8 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95% as obsereved by -PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of the Balb/3T3 cell line, the ED50 is <60ng/ml.

Usage

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

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ProSpec-Clusterin Canine, HEK/CYT-618

ProSpec Clusterin Canine, HEK,ProSpec CYT-618,ProSpec产品,ProSpec代理,ProSpec产品目录,ProSpec 细胞因子,ProSpec Cytokines,在 HEK293 细胞中产生的 Clusterin Canine Recombinant 是一种糖基化的多肽链,含有 436 个氨基酸,分子量为 50.72 kDa。 该蛋白在 N 末端融合了 13 个氨基酸的 Flag 标签。

Clusterin Canine, HEK

Clusterin Canine Recombinant, HEK
CYT-618
2µg
10µg
1mg

Catalogue number

CYT-618

Synonyms

CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Glycoprotein 80, Gp80, CLU.

Introduction

Clusterin mRNA and Clusterin protein are shown to increase with androgen treatment. Binding of clusterin to the LDL-Receptor plays a role in the pathogenesis of membranous glomerulonephritis. Clusterin is down regulated in CaP in association with matched benign controls. Clusterin is involved in cellular senescence and tumorigenesis. Clusterin is involved in photo-oxidative cell death pathway. Clusterin is a functional tumor marker for the diagnosis of pediatric large cell lymphoma. Clusterin is activated in low pH. Clusterin is involved in the inhibition of NF-kappaB signaling through stabilization of IkappaBs thus results in suppression of tumor cell motility. N-terminal deletion of clusterin is vital for its alterations of biogenesis in esophageal squamous cell carcinoma.
Clusterin mRNA 和 Clusterin 蛋白显示随着雄激素治疗而增加。 凝聚素与 LDL 受体的结合在膜性肾小球肾炎的发病机制中起作用。 与匹配的良性对照相关,Clusterin 在 CapP 中被下调。 凝聚素参与细胞衰老和肿瘤发生。 凝聚素参与光氧化细胞死亡途径。 Clusterin 是诊断小儿大细胞淋巴瘤的功能性肿瘤标志物。 凝聚素在低 pH 值下被激活。 Clusterin 通过稳定 IkappaB 参与抑制 NF-kappaB 信号传导,因此导致抑制肿瘤细胞运动。 簇蛋白的 N 末端缺失对其在食管鳞状细胞癌中的生物发生改变至关重要。

Description

Clusterin Canine Recombinant produced in HEK293 cells is a glycosylated, Polypeptide chain containing 436 amino acids and having a molecular mass of 50.72 kDa. The protein is fused with 13 amino acid Flag tag at N-Terminus.
The Apolipoprotein-J Canine is purified by proprietary chromatographic techniques.
在 HEK293 细胞中产生的 Clusterin Canine Recombinant 是一种糖基化的多肽链,含有 436 个氨基酸,分子量为 50.72 kDa。 该蛋白在 N 末端融合了 13 个氨基酸的 Flag 标签。
载脂蛋白-J Canine 通过专有的色谱技术进行纯化。

Source

Human Embryonic Kidney 293 Cells.

Physical Appearance

Filtered White lyophilized powder.

Formulation

Canine Clusterin was filtered and lyophilized from 0.5mg/ml solution containing 20mM Tris buffer and 20mM 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
建议加入去离子水配制约 0.5mg/ml 的工作原液,让冻干颗粒完全溶解。 产品不是无菌的! 在用于细胞培养之前,请用适当的无菌过滤器过滤产品。

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.
将冻干蛋白储存在 -20°C。 重组后分装产品以避免重复的冷冻/解冻循环。 重组蛋白可在 4°C 下保存一段时间; 在 4°C 下两周后它没有显示任何变化。

Purity

Greater than 95% as determined by PAGE.

Amino acid sequence

PGDYKDDDDK PAGDQAVSDT ELQEMSTEGS KYINKEIKNA LKGVKQIKTL IEQTNEERKS LLSNLEEAKK KKEDALNDTK DSETKLKASQ GVCNDTMMAL WEECKPCLKQ TCMKFYARVC RSGSGLVGHQ LEEFLNQSSP FYFWMNGDRI DSLLENDRQQ THALDVMQDS FNRASSIMDE LFQDRFFTRE PQDTYHYSPF SLFQRRPFFN PKFRIARNII PFPRFQPLNF HDMFQPFFDM IHQAQQAMDV NLHRIPYHFP IEFPEEDNRT VCKEIRHNST GCLKMKDQCE KCQEILSVDC SSNNPAQVQL RQELSNSLQI AEKFTKLYDE LLQSYQEKMF NTSSLLKQLN EQFSWVSQLA NLTQSEDPFY LQVTTVGSQT NVPVGFT KVVVKLFDSD PITVMIPEAV SRNNPKFMET VAEKALQEYRQKHREE.

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产品,ProSpec代理,ProSpec产品目录,ProSpec 细胞因子,ProSpec Cytokines

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ProSpec-BMP 2 Human, HEK/CYT-080,Bone Morphogenetic protein-2 Human Recombinant, HEK

ProSpec BMP 2 Human, HEK,CYT-080,Bone Morphogenetic protein-2 Human Recombinant HEK,ProSpec BMP 2 Antibody,冻干的 BMP2 虽然在室温下可稳定保存 3 周,但应在 -18°C 以下干燥储存。 复溶后,BMP-2 应在 4°C 下储存 2-7 天,以备将来在 -18°C 以下使用。

BMP 2 Human, HEK

Bone Morphogenetic protein-2 Human Recombinant, HEK
CYT-080
ProSpec-BMP 2 Human, HEK/CYT-080 2µg
ProSpec-BMP 2 Human, HEK/CYT-080 10µg
ProSpec-BMP 2 Human, HEK/CYT-080 100µg

Catalogue number

CYT-080

Synonyms

BMP-2, BMP2A.

Introduction

BMP2 belongs to the transforming growth factor-beta superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia ossificans progressiva.
BMP2属于转化生长因子-β超家族。 骨形态发生蛋白诱导骨形成。 BMP2 是进行性骨化纤维发育不良的常染色体显性遗传病的候选基因。

Description

BMP-2 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 28kDa due to glycosylation. The BMP2 is purified by proprietary chromatographic techniques.

在 HEK 细胞中产生的 BMP-2 Human Recombinant 是一种糖基化的二硫键连接的同型二聚体,由于糖基化,其分子量范围为 28kDa。 BMP2 通过专有的色谱技术进行纯化。

Source

HEK.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The BMP2 was lyophilized from 0.67mg/ml in 2xPBS + 6% ethanol.

Solubility

It is recommended to reconstitute the lyophilized BMP-2 in sterile 4mM HCl containing 0.1% endotoxin-free recombinant HSA.

Stability

Lyophilized BMP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-2 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.
冻干的 BMP2 虽然在室温下可稳定保存 3 周,但应在 -18°C 以下干燥储存。 复溶后,BMP-2 应在 4°C 下储存 2-7 天,以备将来在 -18°C 以下使用。
对于长期储存,建议添加载体蛋白。
请防止冻融循环。

Purity

Greater than 95.0% as determined by analysis by -PAGE.

Biological Activity

The specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line was found to be 6.53ng/ml.

Amino acid sequence

QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.

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-GH Bovine

  • Description
  • GH Bovine

  • Growth Hormone Bovine Recombinant
  • CYT-636

Catalogue number

CYT-636

Synonyms

BGH, BST, rBGH, rBST, Bovine Somatotropin, Bovine GH, Growth hormone, GH1.

Introduction

GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

Description

Growth Hormone Bovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 21.8 kDa.
The GH Bovine Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The Bovine Growth Hormone protein was lyophilized from a concentrated solution with 4.5mM NaHCO3 adjusted to pH 8-9.

Solubility

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

Stability

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

Purity

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

Amino acid sequence

1      afpamslsgl fanavlraqh lhqlaadtfk efertyipeg qrysiqntqv 
51    afcfsetmpa ptgkneaqqk sdlellrisl lliqswlgpl qflsrvftns 
101  lvfgtsdrvy eklkdleegi lalmreledg tprrgqilkq tydkfdtnmr 
151  sddallknyg llscfrkdlh ktetylrvmk crrfgeasca f

Biological Activity

The activity as determined by the PDFP13B9 cells stably transfected with rabbit GH receptors. Bovine GH is also capable of forming a 1:2 complex with the recombinant ovine growth hormone receptor extracellular domain .

Protein content

UV spectroscopy at 280 nm using the absorbency value of 0.63 as the extinction coefficient for a 0.1% solution. This value is calculated by the PC GENE computer analysis program of protein sequences.

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-GH Carp

  • Description
  • GH Carp

  • Growth Hormone Carp Recombinant
  • CYT-297

Catalogue number

CYT-297

Synonyms

GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

Introduction

Growth-Hormone is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

Description

Growth Hormone Carp Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids & having a molecular mass of 21,408 Dalton.
Growth Hormone Carp is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The GH Carp was lyophilized from a concentrated solution with 0.3% NaHCO3 adjusted to pH 8.

Solubility

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

Stability

Lyophilized Growth Hormone Carp recombinant although stable at room temperature for 3 weeks, should be stored desiccated below
-18°C. Upon reconstitution Growth Hormone Carp 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 SEC-HPLC.
Analysis by -PAGE.

Amino acid sequence

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

Biological Activity

Carp GH is biologically active in rat 3T3 F442A preadipocytes, though its activity is 15-fold lower compared to bovine GH, but it is equally potent in vivo in promoting carp growth . Furthermore, carp GH forms 1:2 complex with the extra cellular domain of ovine growth hormone receptor.

References

Title:Growth Hormone Promotes Hair Cell Regeneration in the Zebrafish Inner Ear following Acoustic Trauma.
Publication:Sun H, Lin C-H, Smith ME Growth Hormone Promotes Hair Cell Regeneration in the Zebrafish Inner Ear following Acoustic Trauma. PLoS ONE 6: e28372. doi:10.1371/journal.pone.0028372
Link:http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0028372

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-GH Chicken

  • Description
  • GH Chicken

  • GH Chicken Recombinant
  • CYT-430

Catalogue number

CYT-430

Synonyms

GH1, GH, GHN, GH-N, hGH-N,Pituitary GH, GH 1, 

Introduction

GH is a member of the prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the GH locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five GHs, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the GH locus. Mutations in or deletions of the gene lead to GH deficiency and short stature.

Description

GH Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids with an additional Ala at its N-terminus and having a molecular mass of 22255 Dalton.
GH Chicken recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.3% NaHCO3 adjusted to pH 8.

Solubility

It is recommended to reconstitute the lyophilized GH Chicken Recombinant in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml and not more than 3 mg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.

Stability

Lyophilized GH Chicken although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and filter sterilization GH can be stored at 4°C for several weeks. At lower concentration addition of a carrier protein is recommended.
Please prevent freeze-thaw cycles.

Purity

Greater than 99.0% as determined by:
Analysis by -PAGE gel.
Analysis by SEC-HPLC.

Amino acid sequence

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

Biological Activity

GH Chicken Recombinantis fully biologically active in homologous assays and in PDF-P1 3B9 cells stably transfected with rabbit GH receptors.

Protein content

Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.75 as the extinction coefficient for a 0.1% solution at pH 8.0 This value is calculated by the PC GENE computer analysis program of protein sequences .
2. Analysis by RP-HPLC, using a calibrated solution of GH as a Reference Standard.

Usage

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

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ProSpec-GH Denis

  • Description
  • GH Denis

  • GH Denis Recombinant
  • CYT-498

Catalogue number

CYT-498

Synonyms

GH1, GH, GHN, GH-N, hGH-N,Pituitary GH, GH 1.

Introduction

GH is a member of the prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the GH locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five GHs, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the GH locus. Mutations in or deletions of the gene lead to GH deficiency and short stature.

Description

GH Denis Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids and having a molecular mass of 21810 Dalton.
GH is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.0045mM NaHCO3.

Solubility

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

Stability

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

Purity

Greater than 97.0% as determined by:
Analysis by SEC-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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  • HGH Antibody
  • GH Human, HEK
  • GH Porcine
  • GH Chicken
  • GH Rat
  • GH Human
  • GH Mahi Mahi
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  • GH Rabbit
  • GH Ovine
  • GH Mouse
  • GH Carp
  • GH Gilthead Seabream
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ProSpec-GH Gilthead Seabream

  • Description
  • GH Gilthead Seabream

  • Growth Hormone Gilthead Seabream Recombinant
  • CYT-529

Catalogue number

CYT-529

Synonyms

GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

Introduction

GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

Description

Somatotropin Gilthead Seabream Recombinant Sparus Aurata produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.4 kDa.
The Gilthead Seabream Growth-Hormone Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.02% NaHCO3.

Solubility

It is recommended to reconstitute the lyophilized Growth-Hormone Gilthead Seabream in 0.4% NaHCO3 or water adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

Stability

Lyophilized Growth-Hormone Gilthead Seabream although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

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

Biological Activity

Binding assays of the 125I-labeled gilthead seabream GH to dolphin fish liver microsomal fraction resulted in high specific binding characterized by a Ka of 1.93 nM and a Bmax of 540 fmol/mg microsomal fraction protein. Recombinant gilthead seabream Growth Hormone, like ovine placental lactogen, exhibited growth-stimulating activity when applied orally to Sparus aurata larvae or intraperitoneally to juvenile fish.

Amino acid sequence

AQPITDGQRLFSIAVSRVQHLHLLAQRLFSDFESSLQTEEQPQLNKIFLQ

DFCNCDYIISPIDKHETQRSSVLKLLSISYRLVESWEFPSRSLSGGSAPR

NQISPKLSELKTGIHLLIRANEDGAEIFPDRSALQLAPYGNYYQSLGTDE

SLRRTYELLACFKKDMHKVETYLTVAKCRLSPEANCTL

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

  • GH Denis
  • GH Human, HEK
  • HGH Antibody
  • GH Porcine
  • GH Chicken
  • GH Rat
  • GH Mahi Mahi
  • GH Human
  • GH Zebrafish
  • GH Rabbit
  • GH Ovine
  • GH Carp
  • GH Mouse
  • GH Bovine
  • GH Rainbow Trout

ProSpec-GH Human

  • Description
  • GH Human

  • Growth Hormone Human Recombinant
  • CYT-202

Catalogue number

CYT-202

Synonyms

GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

Introduction

GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

Description

GH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids and having a molecular mass of 22kDa. Growth Hormone is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

GH protein lyophilized from a 0.2µm filtered concentrated solution with 20mM PB, pH 7.0 and 3% Mannitol.

Solubility

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

Stability

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

Purity

Greater than 98.0% as determined by -PAGE.

Amino acid sequence

FPTIPLSRLF DNAMLRAHRL HQLAFDTYQE FEEAYIPKEQ KYSFLQNPQT SLCFSESIPT PSNREETQQK SNLELLRISL LLIQSWLEPV QFLRSVFANS LVYGANV YDLLKDLEEG IQTLMGRLED GSPRTGQIFK QTYSKFDTNS HNDDALLKNY GLLYCFRKDM DKVETFLRIV QCRSVEGSCG F.

Biological Activity

The ED50 was determined by the proliferation assay of rat lymphoma NB2-11 cells and was found to be less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.

References

Title:Growth Hormone-Releasing Hormone Neurons in the Arcuate Nucleus of the Hypothalamus Are Decreased in Transgenic Rats Whose Expression of Ghrelin Receptor Is Attenuated: Evidence that Ghrelin Receptor Is Involved in the Up-Regulation of GHRH Expression in the Arc.
Publication:Published online before print May 25, 2006, doi: 10.1210/en.2005-1619 Endocrinology September 1, 2006 vol. 147 no. 9 4093-4103.
Link:http://endo.endojournals.org/content/147/9/4093.full

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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