Human EGF Recombinant Protein (RPES4398)

Human EGF Recombinant Protein

EGF is one of the founding members of the EGF-family of proteins. The structural and functional features of this protein family are extremely comparable. EGF has 9 EGF-like domains and 9 LDL-receptor class B repeats. The human EGF protein is a 6045-Da molecule with 53 amino acid residues and three intramolecular disulfide bonds. EGF has first isolated from the mouse submandibular gland as a low-molecular-weight polypeptide. However, it is now present in many human tissues, including the submandibular and parotid glands. Epidermal growth factor (EGF) can be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is an important protein that promotes epidermal and epithelial cell growth in vivo and in vitro. It causes cellular mitosis, differentiation, and survival. Salivary EGF, which is also regulated by dietary inorganic iodine, has an important physiological function in maintaining oro-esophageal and gastric tissue integrity. Epidermal growth factor (EGF) binds to the epidermal growth factor receptor with high affinity and activates the intrinsic protein-tyrosine kinase activity of the receptor. Tyrosine kinase activity is responsible for the activation of a signal transduction pathway that leads to several cellular biochemical changes, such as increases in intracellular calcium levels, glycolysis and protein synthesis, and increased gene expression for certain genes including the gene for EGFR - all of which lead to DNA synthesis and cell proliferation. Human EGF Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.