Tyrosine Kinases / Adaptors
| CSTコード |
包装 |
希望納入価格（円） |
国内在庫  |
ご登録代理店情報 カスタマー情報にご登録いただいた代理店を表示しています。
ご登録代理店の変更は こちら。 |
| #3124S | 100 μL | 57,000 | |
|
PDGFR-b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。
| | |
-
3124:
-
Immunoprecipitation
Western Blotting
| 用途 (希釈倍率) | |
| ウェスタンブロッティング (1:1,000)、免疫沈降 (1:50) |
| 特異性・感度 | |
| 内在性レベルのTyr1009 がリン酸化されたPDGF Receptor βタンパク質を検出します。この抗体は他の活性化したPDGF Receptor ファミリータンパク質及び他の活性化したチロシンキナーゼとも弱く交差反応すると思われます。 |
| 使用抗原 | |
| ヒトPDGF Receptor βタンパク質のTyr1009 周辺領域 (合成リン酸化ペプチド) |
Western Blotting
Western blot analysis of cell extracts from NIH/3T3 cells unstimulated or stimulated with PDGF-BB (100 ng/ml for 5 min), using Phospho-PDGF Receptor-β (Tyr1009) (42F9) Rabbit mAb (upper) or PDGF receptor-β (2B3) Mouse mAb #3175 (lower).
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). PDGF Receptor α homodimers bind all PDGF isoforms except those containing PDGF D. PDGF Receptor β homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGFα/β receptor 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).
Activation of the PDGFRβ leads to autophosphorylation on a number of tyrosine residues, including Tyr1009. Mutation analysis has shown that PDGF-stimulated PLCγ signaling is dependent on autophosphorylation of the PDGFRβ at Tyr1009 and Tyr1021 (9). Phosphorylated Tyr1009 also serves as a binding site for SHP-2, a SH2 domain-containing tyrosine phosphatase that is tyrosine-phosphorylated by PDGFRβ (10).
-
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.
-
Rönnstrand, L. et al. (1992)
EMBO J.
11, 3911-3919.
-
Rönnstrand, L. et al. (1999)
Oncogene
18, 3696-3702.
