Angiogenesis
- Angiogenesis
PhosphoSitePlus®：
PDGFRa
- 推奨プロトコール
Phospho-PDGF Receptor α (Tyr754) (23B2) Rabbit mAb |
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| CSTコード | 包装 | 希望納入価格 (円) |
国内在庫  2012年2月9日15時20分 現在 |
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| #2992S | 100 μL | 57,000 | ログインすると国内在庫状況がご確認いただけます。
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| #2992P | 40 μL for Custom Sampler Kit |  Custom Antibody Sampler Kitの構成品を選択できます。 5本以上を選択し、ページ右上のCartから製品確定書を発行してください。 尚、構成品の単品販売は致しておりません。 |
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2992 の推奨プロトコール 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。 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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| 用途（希釈倍率） | |
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| ウエスタンブロッティング(1:1,000)、免疫沈降(1:50) |
| 種交差性 | |
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| ヒト、マウス |
| 特異性・感度 | |
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| 内在性レベルのTyr754 がリン酸化されたPDGF Receptor αを検出します。PDGF Receptor βとは交差しません。 |
| 検出タンパク質の分子量 | |
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| 198 kDa |
| 使用抗原 | |
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| ヒトのPDGF Receptor αのtyr754 周辺領域（合成ペプチド） |
| 抗体の由来 | |
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| ウサギ |
| 貯法 | |
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| -20℃ |
| 社内データ |
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Western Blotting
Phospho-PDGF Receptor α (Tyr754) (23B2) Rabbit mAb specifically binds to tyrosine phosphorylated PDGF receptor α, but not other phosphorylated tyrosine kinases. Western blot analysis of of extracts from cells expressing different activated tyrosine kinase proteins, using Phospho-PDGF Receptor α (Tyr754) (23B2) Rabbit mAb (upper) or Phospho-Tyrosine Mouse mAb (P-Tyr-100) #9411 (lower).
| バックグラウンド |
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The proteins of the platelet derived growth factor (PDGF) family exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor α (PDGFRα) and PDGF receptor β (PDGFRβ). PDGFRα and PDGFRβ share 75% to 85% sequence homology between their two intracellular kinase domains while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRα homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRβ homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor α/β binds PDGF B, C, and D homodimers as well as the PDGF AB heterodimer (2). PDGFRα and PDGFRβ can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules such as Grb2, Src, GAP, PI3 kinase, PLCγ, and Nck. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRβ is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRβ (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRβ (7). Tyr740 is also required for PDGFRβ-mediated PI3 kinase activation (8).
Interestingly, PDGFR-alpha was found to be phosphorylated at an additional tyrosine residue, Tyr754, in a heterodimeric complex as compared to the alpha-alpha homodimer. Phosphorylation of this tyrosine residue permits the binding of a specific signal-transducing protein, and thereby initiates signaling pathway(s) from the beta-alpha heterodimer, which are dinstinct from those initiated via homodimeric receptor complexes (8).
- Deuel, T.F. et al. (1988) Biofactors 1, 213-217.
- Bergsten, E. et al. (2001) Nat. Cell Biol. 3, 512-516.
- Betsholtz, C. et al. (2001) Bioessays 23, 494-507.
- Coughlin, S.R. et al. (1988) Prog. Clin. Biol. Res. 266, 39-45.
- Ostman, A. and Heldin, C.H. (2001) Adv. Cancer Res. 80, 1-38.
- Panayotou, G. et al. (1992) EMBO J. 11, 4261-4272.
- Ramalingam, K. et al. (1995) Bioorg. Med. Chem. 3, 1263-1272.
- Kashishian, A. et al. (1992) EMBO J. 11, 1373-1382.
- Rupp, E. et al. (1994) Eur J Biochem 225, 29-41.
- Soroceanu, L. et al. (2008) Nature 455, 391-5.
| 使用例 | |
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本製品は試験研究用です。