Epidermal Growth Factor (EGF), human recombinant

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Background

Human epidermal growth factor (EGF) is a member of the EGF-family and plays an important role in the regulation of cell growth, proliferation, and differentiation through binding to its receptor EGFR. The EGF precursor exists as a membrane-bound protein which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. Epidermal growth factor exists in human platelets, macrophages, urine, saliva, milk, and plasma. EGF in salivary has biological effects include inhibition of gastric acid secretion, healing of oral and gastroesophageal ulcers, stimulation of DNA synthesis and mucosal protection from intraluminal injurious factors such as bile acids, gastric acid, trypsin, pepsin and physical, chemical and bacterial agents. The inhibition of EGF can reduce cancer risk. Recombinant human EGF is a 6.2 kDa protein containing 53 amino acid residues. This recombinant human EGF has an N-terminal His-tag preceding the 53 amino acid sequence (MW = 8.5 kDa)