Recombinant Human EGF

Recombinant Human Epidermal Growth Factor (EGF) is a single non-glycosylated polypeptide chain containing 53 amino acids. Epidermal Growth Factor (EGF) 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. Human EGF was isolated from urine based on its inhibitory effect on gastric secretion and named urogastrone, accordingly. EGF 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 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the trans-membrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active.

Lyophilized from a 0.2 um filtered concentrated solution in PBS, pH 7.4.

Centrifuge vial prior to opening. Add sterile distilled water or aqueous buffer to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.

> 1.0 x 10E7 IU/mg