Phospho-EGFR (Tyr1068) (Clone: E5) rabbit mAb

The epidermal growth factor receptor (EGFR; ErbB-1; HER1 in humans) is a transmembrane protein that is a receptor for members of the epidermal growth factor family (EGF family) of extracellular protein ligands (1) . EGFR (rbB-1) is closely related to other members of the ErbB family of receptors: HER2/neu (ErbB-2), HER3 (ErbB-3) and HER4 (ErbB-4) . In many cancer types, mutations affecting EGFR expression or activity could result in cancer (2) . Overexpression of EGFR is associated with the development of a wide variety of tumors. Interruption of EGFR signaling, either by blocking EGFR binding sites on the extracellular domain of the receptor or by inhibiting intracellular tyrosine kinase activity, can prevent the growth of EGFR-expressing tumors and improve the patient's condition. EGFR is activated by the binding of its ligands including EGF and dimerization stimulates its intrinsic intracellular protein-tyrosine kinase activity. Activation of EGFR leads to autophosphorylation of tyrosine (Tyr) residues; Tyr992, Tyr1045, Y1068, Tyr1148, and Tyr1173 in the C-terminal domain.