epitope corresponding to a short amino acid sequence containing phosphorylated Tyr 1068 of EGF receptor of mouse origin
recommended for detection of Tyr 1068 phosphorylated EGF receptor of mouse and human origin by WB, IP, IF and ELISA; also reactive with additional species, including bovine
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 (Tyr 1092m) Product Citations
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p-EGFR (Tyr 1092m)
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p-EGFR (Tyr 1092m): sc-16803. Western blot analysis of EGFR phosphorylation in untreated (A) and EGF treated (B) A-431 whole cell lysates.