raised against an EGFR phosphopeptide of human origin
recommended for detection of Tyr 845 phosphorylated EGFR of mouse, rat and human origin by WB and IP; non cross-reactive with the non-phosphorylated EGFR nor with unrelated Tyrosine-phosphorylated proteins
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 (12A3) Product Citations
See how others have used p-EGFR (12A3): sc-57542 antibody and or p-EGFR (12A3) antibody conjugates.
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p-EGFR (12A3)
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p-EGFR (12A3): sc-57542. Western blot analysis of EGFR phosphorylation in non-stimulated (A), EGF stimulated (B) and pervanadate treated (C) Hep G2 whole cell lysates.
p-EGFR (12A3): sc-57542. Western blot analysis of EGFR phosphorylation in non-stimulated (A), EGF-stimulated (B) and pervanadate treated (C) A549 whole cell lysates.
