Human EGFR Antibody

Epidermal Growth Factor Receptor (EGFR), also named erythroblastic leukemia viral oncogene homolog 1 (ErbB1), is a member of the type I receptor tyrosine kinase superfamily. The epidermal growth factor receptor (EGFR) subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as HER1, ErbB1or ErbB), ErbB2 (Neu, HER2), ErbB3 (HER3), and ErbB4 (HER4). All family members are type I transmembrane glycoproteins that have an extracellular domain with two ligand binding cysteine rich domains, separated by a spacer region, and a cytoplasmic domain with a membrane proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGFR geneencodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 alpha, in the absence of a coreceptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR can also be recruited to form heterodimers with ligand-activated ErbB3 or ErbB4. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis (1 ‑ 3).