Human EGF/Epidermal Growth Factor (Fc Tag) recombinant protein

Human EGF/Epidermal Growth Factor (Fc Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. EGF contains 9 EGF-like domains and 9 LDL-receptor class B repeats. Human EGF is a 6045-Da protein with 53 amino acid residues and three intramolecular disulfide bonds. As a low-molecular-weight polypeptide, EGF was first purified from the mouse submandibular gland, but since then it was found in many human tissues including submandibular gland, parotid gland. It can also be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is a growth factor that stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. It results in cellular proliferation, differentiation, and survival. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. EGF acts by binding with high affinity to epidermal growth factor receptor on the cell surface and stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity, in turn, initiates a signal transduction cascade that results in a variety of biochemical changes within the cell - a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR - that ultimately lead to DNA synthesis and cell proliferation.

Pro-epidermal growth factor

HOMG4; AI790464; URG; EGF

P01133

EGF

Human Cells

A DNA sequence encoding the mature soluble form of human EGF (NP_001954.2) (Asn 971-Arg 1023) was fused with the Fc region of human IgG1 at the N-terminus.

Human

The recombinant human Fc/EGF chimera is a disulfide-linked homodimeric protein. The reduced monomer consists of 290 amino acids and has a calculated molecular mass of 33 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhFc/EGF monomer is approximately 37 kDa due to the glycosylation.

> 90 % as determined by SDS-PAGE

Measured in a cell proliferation assay using Balb/C 3T3 mouse embryonic fibroblast cells.
The ED₅₀ for this effect is typically 0.1-0.6 ng/mL.