CST, 2235S, Phospho-EGF Receptor (Tyr992) Antibody

Polyclonal Antibody for studying EGFR (Tyr1016) phosphate. Validated for Western Blotting,Immunohistochemistry (Paraffin). Available in 3 sizes. Highly specific and rigorously validated in-house, Phospho-EGF Receptor (Tyr992) Antibody (CST #2235) is ready to ship. Product Usage Information Western Blotting: 1:1000 Immunohistochemistry (Paraffin): 1:50 - 1:200 Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at -20°C. Do not aliquot the antibody. Protocol Available protocols: Western Blotting, Immunohistochemistry (Paraffin) Specificity / Sensitivity Phospho-EGF Receptor (Tyr992) Antibody detects endogenous EGF receptor only when phosphorylated at tyrosine 992. This antibody may cross-react with other activated EGF receptor family members (e.g. ErbB2). Species Reactivity: Human, Mouse, Monkey Source / Purification Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr992 of human EGF receptor. Antibodies are purified by protein A and peptide affinity chromatography. Background The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). 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 (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). 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; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10). Alternate Names avian erythroblastic leukemia viral (v-erb-b) oncogene homolog; cell growth inhibiting protein 40; cell proliferation-inducing protein 61; EGF receptor; EGFR; Epidermal growth factor receptor; epidermal growth factor receptor (erythroblastic leukemia viral (v-erb-b) oncogene homolog, avian); epidermal growth factor receptor tyrosine kinase domain; erb-b2 receptor tyrosine kinase 1; ERBB; ERBB1; HER1; mENA; NISBD2; PIG61; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1 Specification REACTIVITY: H M Mk SENSITIVITY: Endogenous MW (kDa): 175 SOURCE: Rabbit