Epidermal growth factor (EGF) stimulates the proliferation and differentiation of a wide variety of cells of ectodermal and mesodermal origin, and is a constituent of many serum-free media formulations. It has been used in the cell differentiation assay.
Recombinant Epidermal Growth Factor, human (hEGF), is produced in E. coli and purified by standard chromatographic techniques. It is a 100μg white lyophilizate, filtered through 0.2μm pore size membrane, recombinant from E. coli.
Epidermal growth factor (EGF) is a small mitogenic polypeptide which is present in many mammalian species and is distributed throughout a wide number of tissues and body fluids EGF is produced in the tubular cells of the submaxillary gland of the mouse, in the acinar cells of the human submaxillary gland, and in the human duodenal glands.
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. 37 amino acids of the 53 amino acids comprising the longer urogastrone (human EGF) and mouse EGF are common to both peptides (70% homology) and the three disulfide bonds are formed in the same relative positions. The biological activity of human EGF is similar to that of mouse EGF. The cellular receptor for EGF is the best understood growth factor receptor. The oncogene v-erbB codes for a product homologous to a portion of the EGF receptor in which the EGF-binding domain has been deleted. Evidence exists suggesting that this truncation of the EGF receptor may lead to constitutive activation without requirement for ligand binding.
EGF stimulates the proliferation and differentiation of awide variety of cells of ectodermal and mesodermal origin (e.g., fibroblasts, glial cells, keratinocytes, epithelial cells, endothelial cells, chondrocytes). EGF is a constituent of many serum-free media formulations for a variety of cells.
