Tyrosine Kinases / Adaptors
| CSTコード |
包装 |
希望納入価格(円) |
国内在庫  |
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| #3056S | 100 μL | 57,000 | |
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EGFR抗体製品一覧
推奨プロトコール
最適な結果を得るために:Cell Signaling Technology (CST) 社は、各製品の推奨プロトコールを使用することを強くお薦めいたします。
推奨プロトコールはCST社内試験の徹底的なバリデーションに基づいて作成されておりますので、正確かつ再現性の高い結果が得られます。
注:各製品に最適化されたプロトコールをリンクしています。
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3056:
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Western Blotting
| 用途(希釈倍率) | |
| ウェスタンブロッティング(1:1,000) |
| 特異性・感度 | |
| 内在性レベルのThr669 がリン酸化されたEGF Receptor タンパク質を検出します。ErbB2 タンパク質など、他の活性型EGF Receptor ファミリータンパク質とは交差しません。 |
| 使用抗原 | |
| ヒトのEGF Receptor タンパク質のThr669 周辺領域(合成リン酸化ペプチド) |
| ※括弧付きの動物種は配列が100%相同であるため反応すると推定されます。 |
Western Blotting
Western blot analysis of extracts of A431 cells, untreated or stimulated with EGF, using Phospho-EGF Receptor (Thr669) Antibody (upper) or EGF Receptor Antibody #2232 (lower).
The epidermal growth factor (EGF) receptor is a 170 kDa 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 c-Cbl, an adaptor protein that leads 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) provides 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 is a major phosphorylation site on EGF receptor after EGF stimulation. It is phosphorylated by p38 MAP kinase (11). Phosphorylation of the EGF receptor at Thr669 may be involved in regulation of ligand induced receptor internalization by interacting with downstream specific EGF receptor tyrosine kinase substrate(s) (11).
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