The epidermal growth factor (EGF) receptor is a 170 kDa transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling and lysosomal degradation . Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme and providing a binding surface for substrate proteins. c-Src is involved in phosphorylation of EGFR at Tyr845. The SH2 domain of PLC? binds at phospho-Tyr992, resulting in activation of PLC?-mediated downstream signaling. Phosphorylation of EGFR at Tyr1045 creates a major docking site for c-Cbl, an adaptor protein that leads to receptor ubiquitination and degradation following EGFR activation. The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068. A pair of phosphorylated residues (Tyr1148 and Tyr1173) provides a docking site for the SHC scaffold protein, with both sites involved in MAP kinase signaling activation. Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutations to either of these serines results in upregulated EGFR tyrosine autokinase activity.

The antibody specifically detects phosphorylated protein derived from A431 cell lysates at various concentrations. In both ELISA and EGFR, this antibody shows no cross-reactivity with other unrelated protein.

12 months from the date of shipment when stored properly.