EGFR Antibody

WB 1:500-1:2000

Store at -20C/1 year

A synthesized peptide derived from human EGFR

EGFR is a receptor tyrosine kinase. Receptor for epidermal growth factor (EGF) and related growth factors including TGF-alpha, amphiregulin, betacellulin, heparin-binding EGF-like growth factor, GP30 and vaccinia virus growth factor. Is involved in the control of cell growth and differentiation. . A single-pass transmembrane tyrosine kinase. Ligand binding to this receptor results in receptor dimerization, autophosphorylation (in trans), activation of various downstream signaling molecules and lysosomal degradation. Can be phosphorylated and activated by Src. Activated EGFR binds the SH2 domain of phospholipase C-gamma (PLC-gamma), activating PLC-gamma-mediated downstream signaling. Phosphorylated EGFR binds Cbl, leading to its ubiquitination and degradation. Grb2 and SHC bind to phospho-EGFR and are involved in the activation of MAP kinase signaling pathways. Phosphorylation on Ser and Thr residues is thought to represent a mechanism for attenuation of EGFR kinase activity. Overexpressed in breast, head and neck cancers, correlating with poor survival. Activating somatic mutations seen in lung cancer, corresponding to minority of patients with strong response to EGFR inhibitor Iressa (gefitinib). Mutations and amplification also seen in glioblastoma, and upregulation seen in colon cancer and neoplasms. In xenografts, inhibitors synergized with cytotoxic drugs in inhibition of many tumor types. Inhibitors: Iressa/ZD1839, Erbitux, Tarceva, and lapatinib. Four alternatively spliced isoforms have been described.

EN0035878