Recombinant EGF, Human 
Datasheet
COA
MSDS
SHIP
Recombinant :
Recombinant EGF, Human Source :
Escherichia coli. Molecular Weight :
6.2kDa, observed by reducing SDS-PAGE. Purity :
> 95% by SDS-PAGE analysis. Biological Activity :
ED50 <0.6ng/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblasts in serum-free medium and CellTiter-Glo cell viability assay, corresponding to a specific activity of >1.7 x 10ˆ6 units/mg. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against 10 mM PB, pH 7.0. AA Sequence :
MNSDSECPL SHDGYCLHDG VCMYIEALDK YACNCVVGYI GERCQYRDLK WWELR Endotoxin :
Less than 0.1 ng/µg (1 EU/μg) determined by LAL test Reconstitution :
Reconstituted in ddH2O at 100 μg/ml. Storage :
Lyophilized recombinant human Epidermal Growth Factor (rhEGF) remains stable up to 12 months at -80°C from date of receipt. Upon reconstitution, rhEGF should be stable up to 4 weeks at 4°C or up to 6 months at -20°C. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only. Description :
Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through a receptor known as c-erbB, which is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). Recombinant human EGF is a 6.2 kDa globular protein containing 53 amino acid residues including 3 intramolecular disulfide-bonds. Recombinant human Epidermal Growth Factor (rhEGF) produced in E. coli is a non-glycosylated polypeptide chain of 54 amino acids. A fully biologically active molecule, rhEGF has a molecular mass of 6.2kDa analyzed by reducing SDS-PAGE and is obtained by proprietary refolding and chromatographic techniques at GenScript.
Recombinant EGF, Human Source :
Escherichia coli. Molecular Weight :
6.2kDa, observed by reducing SDS-PAGE. Purity :
> 95% by SDS-PAGE analysis. Biological Activity :
ED50 <0.6ng/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblasts in serum-free medium and CellTiter-Glo cell viability assay, corresponding to a specific activity of >1.7 x 10ˆ6 units/mg. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against 10 mM PB, pH 7.0. AA Sequence :
MNSDSECPL SHDGYCLHDG VCMYIEALDK YACNCVVGYI GERCQYRDLK WWELR Endotoxin :
Less than 0.1 ng/µg (1 EU/μg) determined by LAL test Reconstitution :
Reconstituted in ddH2O at 100 μg/ml. Storage :
Lyophilized recombinant human Epidermal Growth Factor (rhEGF) remains stable up to 12 months at -80°C from date of receipt. Upon reconstitution, rhEGF should be stable up to 4 weeks at 4°C or up to 6 months at -20°C. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only. Description :
Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through a receptor known as c-erbB, which is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). Recombinant human EGF is a 6.2 kDa globular protein containing 53 amino acid residues including 3 intramolecular disulfide-bonds. Recombinant human Epidermal Growth Factor (rhEGF) produced in E. coli is a non-glycosylated polypeptide chain of 54 amino acids. A fully biologically active molecule, rhEGF has a molecular mass of 6.2kDa analyzed by reducing SDS-PAGE and is obtained by proprietary refolding and chromatographic techniques at GenScript.
Blocking peptide available as BK0026-1mgP