EGFR (Ser-1142), Phosphospecific Antibody

The epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein with an extracellular ligand-binding domain and a cytoplasmic domain with intrinsic tyrosine kinase activity. The cytoplasmic domain has a C-terminal region with multiple autophosphorylation sites (Tyr-992, 1068, 1086, 1148, and 1173) . These sites are important for downstream signaling and rapid internalization. In addition, EGFR activation leads to c-Src mediated phosphorylation of Tyr-845 and Tyr-1101. The former site is required for mitogenic responses to EGFR activation, while the latter may be an SH2 binding site. Phosphorylation of EGFR on serine and threonine residues is thought to represent a mechanism for regulation of receptor kinase activity and internalization. These sites include a PKC site (Thr-654), CAMKII sites (Ser-1046, 1047, 1057, and 1142), and constitutively phosphorylated sites (Ser-967 and Ser-1002) . Thus, the regulation of EGFR activity involves a complex series of phosphorylation events at multiple sites throughout the intracellular portion of the receptor.

This antibody was cross-adsorbed to unphosphorylated EGFR (Ser-1142) coupled to agarose then Affinity purification using phospho-EGFR (Ser-1142) peptide (without carrier) . The antibody detects a 180 kDa* protein on SDS-PAGE immunoblots of human A431 cells treated with Calyculin A, and does not detect this band after lambda phosphatase treatment. This human EGFR sequence has high homology with rat and mouse EGFR, and is not conserved in other ErbB family members.