raised against an EFGR phosphopeptide of human origin
recommended for detection of Tyr 1173 phosphorylated EGFR of mouse, rat and human origin by WB, IP and IF; non cross-reactive with the non-phosphorylated EGFR nor with unrelated Tyrosine-phosphorylated proteins; also reactive with additional species, including canine
p-EGFR Background Information Epidermal growth factor mediates its effects on cell growth through its inter-action with a cell surface glycoprotein designated the EGF receptor. Binding of EGF or TGF alpha 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. Once activated, EGFR mediates the binding of the phosphotyrosine binding (PTB) domain of GRB2 through direct interactions with Tyr 1068 and Tyr 1086 and through indirect interactions with Tyr 1173 in the Ras signaling pathway. Tyr 1173 of EGFR also functions as a kinase substrate. Phosphorylation of Tyr 992, Tyr 1068 and Tyr 1086 is required for conformational change in the C-terminal tail of the EGF receptor.
p-EGFR (9H2)
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p-EGFR (9H2): sc-57545. Western blot analysis of EGFR phosphorylation in non-stimulated (A), EGF stimulated (B) and pervanadate stimulated (C) A549 whole cell lysates.
