EGFR (phospho-Y992) polyclonal antibody

P00533

Epidermal growth factor mediates its effects on cell growth through its interaction with a cell surface glycoprotein designated the EGF receptor. Binding of EGF or TGFalpha to the EGF receptor activates tyrosine-specific protein kinase activity intrinsic to the EGF receptor. The carboxy-terminal tyrosine residues on EGFR, Tyr 1068 and Tyr 1173, are the major sites of autophosphorylation, which occurs as a result of EGF binding. Phosphorylation of Tyr 992, Tyr 1068 and Tyr 1086 is required for conformational change in the C-terminal tail of the EGF receptorgulates Actin filament accumulation at the plasma membrane and Cdc42 stimulates formation of filopodia.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

p-EGFR (Y992) pAb detects endogenous levels of EGFR protein only when phosphorylated at Tyr992 (removal of the signal peptide).

Immunohistochemistry analysis of paraffin-embedded human breast carcinoma, using p-EGFR (Y992) pAb. The picture on the right is treated with the synthesized peptide.

ca. 175 kDa

Epidermal growth factor receptor, EC=2.7.10.1, Proto-oncogene c-ErbB-1, Receptor tyrosine-protein kinase erbB-1, ERBB, ERBB1, HER1, EGFR