重组人粒细胞集落刺激因子(源自CHO) (rHuCHO-G-CSF)

产品介绍

 

CYT-329 重组人粒细胞集落刺激因子(源自CHO) (rHuCHO-G-CSF)  2μg/10μg/1mg   Prospec

 

 

Background :
  A glycoprotein of MW 20 kDa containing internal disulfide bonds. It induces the survival, proliferation, and differentiation of neutrophilic granulocyte precursor cells and functionally activates mature blood neutrophils. Among the family of colony-stimulating factors, G-CSF is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines.
The synthesis of G-CSF can be induced by bacterial endotoxins , TNF , Interleukin-1 and GM-CSF . Prostaglandin E2 inhibits the synthesis of G-CSF. In epithelial, endothelial, and fibroblastic cells secretion of G-CSF is induced by Interleukin-17 .

 

Description :
  Recombinant Human Granulocyte Colony Stimulating Factor is a glycosylated, polypeptide chain containing 174 amino acids and having a molecular mass of 20 KD.
Human G-CSF is purified by proprietary chromatographic techniques.

 

Physical Appearance:
  Sterile Filtered White lyophilized (freeze-dried) powder.

 

Formulation:
  Human G-CSF was lyophilized from a concentrated (1mg/ml) solution containing 10mM Hydrochloric Acid pH=6.5, 0.4mg tween 20, 100mg mannitol, 160 mg L-arginine, 40 mg phenylalanin and 4mg methionin.
Solubility:
  It is recommended to reconstitute the lyophilized G-CSF in sterile 18MO-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 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 (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

 

Purity:
  Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained.

 

Amino-Acid Sequence :
  The sequence of the first five N-terminal amino acids was determined and was found to be
Thr-Pro-Leu-Gly-Pro.

 

Dimers and aggregates:
  Less than 1% as determined by silver-stained SDS-PAGE gel analysis.

 

Biological Activity:
  ProSpec's G-CSF is fully biologically active when compared to standard. The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is less then 0.1 ng/ml, corresponding to a Specific Activity of 1.27 x 108 IU/mg.

 

Endotoxin:
  Less than 0.1 ng/µg (IEU/µg) of Recombinant Human Granulocyte Colony Stimulating Factor.

 

Protein content:
  G-CSF protein 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% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (InliGenetics).
2. Analysis by RP-HPLC, using a calibrated solution of Recombinant Human Granulocyte Colony Stimulating Factor 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.

 

 

Latest Publications:
  1. Granulocyte colony-stimulating factor and acute myocardial infarction.

JAMA 2006 Oct 25;296(16):1968; auth or reply 1968-9

2. Granulocyte colony-stimulating factor and acute myocardial infarction.

JAMA 2006 Oct 25;296(16):1967-8; author reply 1968-9

3. Autocrine growth by granulocyte colony-stimulating factor in malignant mesothelioma.

Ann Thorac Surg 2006 Nov;82(5):1904-6

4. Granulocyte colony-stimulating factor.

CMAJ 2006 Oct 24;175(9):1095; author reply 1095-6

5. Granulocyte colony-stimulating factor.

CMAJ 2006 Oct 24;175(9):1095; author reply 1095-6

6. Weekly cisplatin, epirubicin, and paclitaxel with granulocyte colony-stimulating factor support vs triweekly epirubicin and paclitaxel in locally advanced breast cancer: final analysis of a sicog phase III study.

Br J Cancer 2006 Oct 23;95(8):1005-12
 

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重组鼠粒细胞克隆刺激因子(rmG-CSF)

产品介绍

 

CYT-410 重组鼠粒细胞克隆刺激因子(rmG-CSF)  2μg/10μg/1mg   Prospec

 

 

Background :
  A glycoprotein of MW 20 kDa containing internal disulfide bonds. It induces the survival, proliferation, and differentiation of neutrophilic granulocyte precursor cells and functionally activates mature blood neutrophils. Among the family of colony-stimulating factors, G-CSF is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines. The synthesis of G-CSF can be induced by bacterial endotoxins , TNF , Interleukin-1 and GM-CSF . Prostaglandin E2 inhibits the synthesis of G-CSF. In epithelial, endothelial, and fibroblastic cells secretion of G-CSF is induced by Interleukin-17 .

 

Description :
  Recombinant Mouse G-CSF produced in E.coli is a single, non-glycosylated, polypeptide chain containing 179 amino acids and having a molecular mass of 19 KD.
Recombinant murine G-CSF is purified by proprietary chromatographic techniques.

 

Physical Appearance:
  Sterile Filtered White lyophilized (freeze-dried) powder.

 

Formulation:
  The protein was lyophilized with no additives.

 

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

 

Stability:
 
  Lyophilized Mouse G-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -180C. Upon reconstitution Recombinant G-CSF should be stored at 40C between 2-7 days and for future use below -180C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

 

Purity:
  Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

 

Amino acid sequence:
  The sequence of the first five N-terminal amino acids was determined and was found to be Met-Val-Pro-Leu-Val.

 

Dimers and aggregates:
  Less than 1% as determined by silver-stained SDS-PAGE gel.

 

Biological Activity:
  ProSpec’s G-CSF is fully biologically active when compared to standard. The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml, corresponding to a Specific Activity of 2 x 107IU/mg.

 

Endotoxin:
  Less than 0.1 ng/µg (IEU/µg) of Mouse G-CSF .

 

Protein content:
  Protein quantitation was carried out by two independent methods:

1. UV spectroscopy at 280 nm using the absorbency value of 0.51 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (InliGenetics).
2. Analysis by RP-HPLC, using a calibrated solution of G-CSF as a Reference Standard.

 

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

 

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重组人粒细胞集落刺激因子(rHuG-CSF)

产品介绍

 

CYT-220 重组人粒细胞集落刺激因子(rHuG-CSF)  2μg/10μg/1mg   Prospec

 

 

Background :
  A glycoprotein of MW 20 kDa containing internal disulfide bonds. It induces the survival, proliferation, and differentiation of neutrophilic granulocyte precursor cells and functionally activates mature blood neutrophils. Among the family of colony-stimulating factors, G-CSF is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines. The synthesis of G-CSF can be induced by bacterial endotoxins , TNF , Interleukin-1 and GM-CSF . Prostaglandin E2 inhibits the synthesis of G-CSF. In epithelial, endothelial, and fibroblastic cells secretion of G-CSF is induced by Interleukin-17 .

 

Description :
  Recombinant Human G-CSF produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8 KD
Recombinant G-CSF is purified by proprietary chromatographic techniques.

 

Physical Appearance:
  Sterile Filtered White lyophilized (freeze-dried) powder.

 

Formulation:
  Recombinant G-CSF was lyophilized after extensive dialysis against 10mM sodium acetate buffer pH= 4.
Solubility:
  It is recommended to reconstitute the lyophilized G-CSF in sterile 18MΩ-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 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 (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

 

Purity:
  Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

 

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

 

Dimers and aggregates:
  Less than 1% as determined by silver-stained SDS-PAGE gel analysis.

 

Biological Activity:
  ProSpec's Recombinant Human Granulocyte-Colony Stimulating Factor is fully biologically active when compared to standard. The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is less then 0.1 ng/ml, corresponding to a Specific Activity of 1 x 108 IU/mg.

 

Endotoxin:
  Less than 0.1 ng/µg (IEU/µg) of G-CSF .

 

Protein content:
  Protein 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% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (InliGenetics).
2. Analysis by RP-HPLC, using a standard solution of recombinant G-CSF as a Reference Standard.

 

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

 

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官方价:
¥10.00
产品编号:
TB21070501-7#
品牌:
其它
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型号规格:
TB21070501-10#/10号 100个/包  TB21070501-3#/3号 100个/包  TB21070501-4#/4号 100个/包  TB21070501-5#/5号 100个/包  TB21070501-7#/7号 100只/包  TB21070501-8#/8号 100只/包  
1
 

    

   

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重组人红细胞生成素-α(rHuEPO-a)

产品介绍

 

CYT-201 重组人红细胞生成素-α(rHuEPO-a)  5ug/50ug   Prospec

 

 

Description :
  Recombinant Human Erythropoietin-alpha is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a single, polypeptide chain containing 165 amino acids and having a predicted molecular mass of 21,000 Dalton and apparent glycosylated molecular mass of 30,400 Dalton.
EPO-alpha is purified by proprietary chromatographic techniques.

 

Physical Appearance:
  Sterile Filtered White lyophilized (freeze-dried) powder.

 

Formulation:
  Recombinant Erythropoietin-alpha was lyophilized after extensive dialysis in 5.8mg sodium citrate, 5.8mg sodium chloride and 0.06mg citric acid.

 

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

 

Stability:
 
  Lyophilized Epoetin Alfa although stable at room temperature for 3 weeks, should be stored desiccated below -18 C. Upon reconstitution EPO 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 (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

 

Purity:
  Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

 

Dimers and aggregates:
  Less than 1% as determined by silver-stained SDS-PAGE gel analysis.

 

Biological Activity:
  ProSpec's Erythropoietin is fully biologically active when compared to standard. The Specific Activity was measured by Normocyth-aemic mice and was found to be 120,000IU/mg.

 

Endotoxin:
  Less than 0.1 ng/µg (IEU/µg) of Epoetin Alfa .

 

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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