Cytoskeletal Signaling
| CSTコード |
包装 |
希望納入価格 (円) |
国内在庫  |
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| #3242S | 100 μL | 46,000 | |
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PAK4抗体製品一覧
3242 の推奨プロトコール
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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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3242:
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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PAK4 タンパク質を検出します。 |
| 使用抗原 | |
| ヒトのPAK4 タンパク質のN末端配列（合成ペプチド） |
Western Blotting
Western blot analysis of extracts from SH-SY5Y, NIH/3T3, C6 and COS cells and guinea pig neutrophils, using PAK4 Antibody.
The p21-activated kinase (PAK) family of serine/threonine kinases is engaged in multiple cellular processes, including cytoskeletal reorganization, MAPK signaling, apoptotic signaling, control of phagocyte NADPH oxidase, and growth factor-induced neurite outgrowth (1,2). Several mechanisms that induce PAK activity have been reported. Binding of Rac/Cdc42 to the CRIB (or PBD) domain near the amino terminus of PAK causes autophosphorylation and conformational changes in PAK (1). Phosphorylation of PAK1 at Thr423 by PDK induces activation of PAK1 (3). Several autophosphorylation sites have been identified, including Ser199 and Ser204 of PAK1 and Ser192 and Ser197 of PAK2 (4,5). Because the autophosphorylation sites are located in the amino-terminal inhibitory domain, it has been hypothesized that modification in this region prevents the kinase from reverting to an inactive conformation (6). Research indicates that phosphorylation at Ser144 of PAK1 or Ser139 of PAK3 (located in the kinase inhibitory domain) affects kinase activity (7). Phosphorylation at Ser21 of PAK1 or Ser20 of PAK2 regulates binding with the adaptor protein Nck (8). PAK4, PAK5, and PAK6 have lower sequence similarity with PAK1-3 in the amino-terminal regulatory region (9). Phosphorylation at Ser474 of PAK4, a site analogous to Thr423 of PAK1, may play a pivotal role in regulating the activity and function of PAK4 (10).
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Knaus, U.G. and Bokoch, G.M. (1998) Int. J. Biochem. Cell Biol. 30, 857-862.
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Daniels, R.H. et al. (1998) EMBO J. 17, 754-764.
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King, C.C. et al. (2000) J. Biol. Chem. 275, 41201-41209.
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Manser, E. et al. (1997) Mol. Cell. Biol. 17, 1129-1143.
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Gatti, A. et al. (1999) J. Biol. Chem. 274, 8022-8028.
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Lei, M. et al. (2000) Cell 102, 387-397.
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Chong, C. et al. (2001) J. Biol. Chem. 276, 17347-17353.
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Zhao, Z. et al. (2000) Mol. Cell. Biol. 20, 3906-3917.
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Abo, A. et al. (1998) EMBO J. 17, 6527-6540.
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Qu, J. et al. (2001) Mol. Cell. Biol. 21, 3523-3533.
PhosphoSitePlus®：
