EGF (human, recombinant; Fc-tagged)

Territorial Availability: Available through Bertin Technologies only in France

• Correlated keywords
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• Product Overview:
  Epidermal growth factor (EGF) is a polypeptide ligand for the EGF receptor (EGFR; Item No. 32026).{53764,53765} It is synthesized as a 1,217 amino acid glycosylated transmembrane precursor protein from which mature, soluble EGF is formed by proteolysis. Mature EGF is a 53-amino acid polypeptide that contains six cysteine residues, which form three intramolecular disulfide bonds essential to the biological activity of EGF. EGF is synthesized in the brain, kidney, pancreas, small intestine, pituitary gland, and submaxillary gland and is found in various bodily fluids, including saliva, cerebrospinal fluid, blood, breast milk, and prostatic fluid.{53765} Binding of EGF to the EGFR induces receptor dimerization, autophosphorylation, and intracellular signaling with roles in cell proliferation. In patients with early Parkinson’s disease and Alzheimer’s disease with amnestic mild cognitive impairment, low plasma EGF levels are predictive of future long-term cognitive decline.{53766} Plasma levels of EGF are reduced in pregnant woman infected with T. cruzi compared with uninfected pregnant controls.{53767} Exogenous application of EGF normalizes cortical GABAergic transmission and improves rotarod performance in the R6/2 transgenic mouse model of Huntington’s disease.{53767} Probiotic administration of E. coli engineered to secrete human EGF induces epithelial barrier restoration in a mouse model of intestinal ulcers.{53769} Immunization with human EGF induces an anti-EGF antibody response and increased survival in mice with EGFR-expressing tumors.{53770} Cayman’s EGF (human, recombinant) protein can be used for cell-based assay applications. This protein is a disulfide-linked homodimer. The reduced monomer, comprised of mature EGF (amino acids 971-1023) fused to human IgG1 Fc at its N-terminus, consists of 290 amino acids and has a calculated molecular weight of 33 kDa. As a result of glycosylation, the monomer migrates at approximately 37 kDa by SDS-PAGE under reducing conditions.