CST, 8808T, Phospho-EGF Receptor (Thr669) (D2F1) Rabbit Monoclonal Antibody

Monoclonal Antibody for studying EGFR (Thr693) phosphate. Validated for Western Blotting,Immunoprecipitation. Available in 2 sizes. Highly specific and rigorously validated in-house, Phospho-EGF Receptor (Thr669) (D2F1) Rabbit Monoclonal Antibody (CST #8808) is ready to ship. Product Usage Information Western Blotting: 1:1000 Immunoprecipitation: 1:200 Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at -20°C. Do not aliquot the antibody. Protocol Available protocols: Western Blotting, Immunoprecipitation Specificity / Sensitivity Phospho-EGF Receptor (Thr669) (D2F1) Rabbit Monoclonal Antibody detects endogenous levels of EGFR protein only when phosphorylated at Thr669. While the literature refers to this residue as Thr669, it is Thr693 of human EGFR (UniProt sequence P00533) and corresponds to Thr695 of mouse EGFR or Thr694 of rat EGFR. Species Reactivity: Human Source / Purification Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr693 of human EGFR protein. 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). Thr669 (equivalent to Thr693 of human EGFR) is phosphorylated by p38 MAP kinase following EGF stimulation (11). Phosphorylation of EGFR at Thr669 may be involved in regulation of ligand induced receptor internalization through interaction with specific downstream EGFR tyrosine kinase substrates (11). 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 SENSITIVITY: Endogenous MW (kDa): 175 Source/Isotype: Rabbit IgG