Epidermal Growth Factor, human, animal component free

Epidermal Growth Factor (EGF) is a small mitogenic polypeptide (∼6 kDa), which is present in many mammalian species and is distributed throughout a wide number of tissues and body fluids.^† Human EGF is identical to β-urogastrone, a polypeptide which was recognized and isolated on the basis of its ability to inhibit gastric acid secretion.^† EGF is a member of a growth factor family, which is characterized by the presence of 6 conserved cysteine motifs that form three disulfide bonds. The location of 3 intrachain disulfide bonds in recombinant human EGF is identical to that of mouse EGF.^† EGF is homologous to a sequence contained in a 19 kDa protein of vaccinia virus,^† which appears to utilize the EGF receptor to gain entry into cell† EGF is mitogenic for a variety of epidermal and epithelial cells, including fibroblasts, glial cells, mammary epithelial cells, vascular and corneal endothelial cells, bovine granulosa, rabbit chondrocytes, HeLa cells, and SV40-3T3 cells.^†

Epidermal growth factor (EGF) is synthesized in Henle′s loop and the distal convoluted tubule in the kidney. It is also produced in salivary glands and duodenum.

Epidermal Growth Factor, human, animal component free has been used:

• as a supplement in in LHC-8 medium to culture liver cell lines
• in the fetal bovine serum (FBS)-Dulbecco′s modified essential medium (DMEM) /F12 medium for primary culture of human glioma cells
• as an additive in the conditional medium of normal fibroblasts (NFs) to study its effect on the migration and invasion of endometrial cancer (EC) cells
• as a component in tumorsphere medium

Epidermal growth factor (EGF) helps to induce cell growth, proliferation and differentiation. It participates in the repairing of renal tissues in the kidney. It promotes the reabsorption of magnesium with the help of the transient receptor potential cation channel 6 (TRMP6). EGF is known to participate in the pathophysiology of drug-induced renal magnesium loss.

1. Carpenter, G., and Cohen, S., Rapid enhancement of protein phosphorylation in A-431 cell membrane preparations by epidermal growth factor. Annu. Rev. Biochem., 48, 193-216 (1979).
2. Gregory, H., Isolation and structure of urogastrone and its relationship to epidermal growth factor. Nature, 257, 325-327 (1975).
3. George-Nascimento, C. et al., Characterization of recombinant human epidermal growth factor produced in yeast. Biochemistry, 27, 797-802 (1988).
4. Todaro, G.J. et al., Transforming growth factors produced by certain human tumor cells: polypeptides that interact with epidermal growth factor receptors. Proc. Natl. Acad. Sci. USA, 77, 5258-5262 (1980).
5. Blomquist, M.C. et al., Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth factors. Proc. Natl. Acad. Sci. USA, 81, 7363-7367 (1984).
6. Eppstein, D.A. et al., Epidermal growth factor receptor occupancy inhibits vaccinia virus infection. Nature, 318, 663-665 (1985).