conserved amino acid sequence: CX7CX4-5CX10-13CXCX8GXRC Where C is cysteine, G is glycine, R is arginine, and X represents any amino acid. This sequence contains six cysteine residues that form three intramolecular disulfide bonds. Disulfide bond formation generates three structural loops that are essential for high-affinity binding between members of the EGF-family and their cell-surface receptors. Interactions Epidermal growth factor has been shown to interact with epidermal growth factor receptor. Medical uses Recombinant human epidermal growth factor, sold under the brand name Heberprot-P, is used to treat diabetic foot ulcers. It can be given by injection into the wound site, or may be used topically. Tentative evidence shows improved wound healing. Safety has been poorly studied. EGF is used to modify synthetic scaffolds for manufacturing of bioengineered grafts by emulsion electrospinning or surface modification methods. Bone regeneration EGF plays an enhancer role on osteogenic differentiation of dental pulp stem cells (DPSCs) because it is capable of increasing extracellular matrix mineralization. A low concentration of EGF (10 ng/ml) is sufficient to induce morphological and phenotypic changes. These data suggests that DPSCs in combination with EGF could be an effective stem cell-based therapy to bone tissue engineering applications in periodontics and oral implantology. History EGF was the second growth factor to be identified. Initially, human EGF was known as urogastrone. Stanly Cohen discovered EGF while working with Rita Levi-Montalcini at the Washington University in St. Louis during experiments researching nerve growth factor. For these discoveries Levi-Montalcini and Cohen were awarded the 1986 Nobel Prize in Physiology or Medicine. References Further reading External links Shaanxi Zhongbang Pharma-Tech Co., Ltd.-Supply of Epidermal Growth Factor EGF at the Human Protein Reference Database . EGF model in BioModels database Growth factors Morphogens