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-alpha 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.
Molecular Weight:
6.2kDa, observed by reducing SDS-PAGE.
Source:
Escherichia coli.
Purity:
> 95% by SDS-PAGE analysis.
Form:
Sterile Filtered White lyophilized (freeze-dried) powder.
