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- mouse monoclonal IgG1, 50 µg/ 0.5 ml
- raised against synthetic phosphopeptide corresponding to amino acid residues surrounding serine 1047 of EGFR of human origin
- recommended for detection of Ser 1047 phosphorylated EGFR of mouse and human origin by WB, IP and IF; also reactive with additional species, including canine
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Ordering Information
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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. |
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p-EGFR(1H9)
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p-EGFR (1H9): sc-57543. Western blot analysis of EGFR phoshorylation in A-431 whole cell lysate.
p-EGFR (1H9): sc-57543. Western blot analysis of EGFR phosphorylation in untreated (A) and lambda protein phosphatase treated (B) SK-OV-3 whole cell lysates.
p-EGFR (1H9): sc-57543. Western blot analysis of EGFR phosphorylation in serum starved Hep G2 whole cell lysate (A) and serum starved PMA-treated (B), Forskolin-treated (C), LPA-treated (D), Sorbit-treated (E), Anisomycin-treated (F), lonomycin-treated (G) and Taxol-treated (H) Hep G2 whole cell lysates.
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