EGFHuman/重组人表皮生长因…

EGFHuman/重组人表皮生长因子
产品简介
详细介绍
  • 参考报价:电议 产地:其他国家 品牌:无 型号:CYT-217 更新时间:2017/2/10

EGF Human/重组人表皮生长因子

产品编号:CYT-217
产品规格:100μg/500μg/1mg
 

Synonyms Urogastrone, URG, EGF.
Introduction Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Description Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6222 Dalton.
The EGF is purified by proprietary chromatographic techniques.
Source Escherichia Coli.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM Phosphate buffer pH-7.4.
Solubility It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100μg/ml, which can then be further diluted to other aqueous solutions.
Stability Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below
-18°C. Upon reconstitution EGF 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 prevent freeze-thaw cycles.
Purity Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Amino acid sequence NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
Biological Activity The ED50, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 10,000,000 Units/mg.
Protein content EGF quantitation was carried out by two independent methods
1. UV spectroscopy at 280 nm using the absorbency value of 2.858 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 (IntelliGenetics).

2. Analysis by RP-HPLC, using a calibrated solution of EGF 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.
Synonyms Urogastrone, URG, EGF.
Introduction Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Description Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6222 Dalton.
The EGF is purified by proprietary chromatographic techniques.
Source Escherichia Coli.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM Phosphate buffer pH-7.4.
Solubility It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100μg/ml, which can then be further diluted to other aqueous solutions.
Stability Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below
-18°C. Upon reconstitution EGF 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 prevent freeze-thaw cycles.
Purity Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Amino acid sequence NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
Biological Activity The ED50, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 10,000,000 Units/mg.
Protein content EGF quantitation was carried out by two independent methods
1. UV spectroscopy at 280 nm using the absorbency value of 2.858 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 (IntelliGenetics).

2. Analysis by RP-HPLC, using a calibrated solution of EGF 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.
Synonyms Urogastrone, URG, EGF.
Introduction Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Description Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6222 Dalton.
The EGF is purified by proprietary chromatographic techniques.
Source Escherichia Coli.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM Phosphate buffer pH-7.4.
Solubility It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100μg/ml, which can then be further diluted to other aqueous solutions.
Stability Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below
-18°C. Upon reconstitution EGF 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 prevent freeze-thaw cycles.
Purity Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Amino acid sequence NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
Biological Activity The ED50, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 10,000,000 Units/mg.
Protein content EGF quantitation was carried out by two independent methods
1. UV spectroscopy at 280 nm using the absorbency value of 2.858 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 (IntelliGenetics).

2. Analysis by RP-HPLC, using a calibrated solution of EGF 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.
Synonyms Urogastrone, URG, EGF.
Introduction Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Description Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6222 Dalton.
The EGF is purified by proprietary chromatographic techniques.
Source Escherichia Coli.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM Phosphate buffer pH-7.4.
Solubility It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100μg/ml, which can then be further diluted to other aqueous solutions.
Stability Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below
-18°C. Upon reconstitution EGF 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 prevent freeze-thaw cycles.
Purity Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Amino acid sequence NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
Biological Activity The ED50, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 10,000,000 Units/mg.
Protein content EGF quantitation was carried out by two independent methods
1. UV spectroscopy at 280 nm using the absorbency value of 2.858 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 (IntelliGenetics).

2. Analysis by RP-HPLC, using a calibrated solution of EGF 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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