Discription：Epidermal Growth Factor was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. It is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit （defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds） in their extracellular domain. EGF is initially synthesized as a 130kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature mouse EGF shares 70％ a.a. sequence identity with mature human EGF. 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. Recombinant Murine EGF is a 6.0kDa globular protein containing 53 amino acid residues, including 3 intramolecular disulfide bonds.
