Ca, cAMP & Lipid Signaling
Phospho-PKA C (Thr197) Antibody
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| CSTコード |
包装 |
希望納入価格 (円) |
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| #4781S | 100 μL | 57,000 | |
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PKA C-alpha抗体製品一覧
4781 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。
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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4781:
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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Thr197 がリン酸化されたPKA C-α、β、γタンパク質を検出します。他の部位がリン酸化されたPKA C タンパク質とは交差しません。 |
| 使用抗原 | |
| PKA C タンパク質のThr197 周辺領域 (合成リン酸化ペプチド) |
Western Blotting
Western blot analysis of extracts from C6 and NIH/3T3 cells, untreated or treated with lambda phosphatase (PPase), using Phospho-PKA C (Thr197) Antibody (upper) or PKA C-alpha Antibody #4782 (lower).
The second messenger cyclic AMP (cAMP) activates cAMP-dependent protein kinase (PKA or cAPK) in mammalian cells and controls many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation (1). Inactive PKA is a heterotetramer composed of a regulatory subunit (R) dimer and a catalytic subunit (C) dimer. In this inactive state, the pseudosubstrate sequences on the R subunits block the active sites on the C subunits. Three C subunit isoforms (C-α, C-β, and C-γ) and two families of regulatory subunits (RI and RII) with distinct cAMP binding properties have been identified. The two R families exist in two isoforms, α and β (RI-α, RI-β, RII-α, and RII-β). Upon binding of cAMP to the R subunits, the autoinhibitory contact is eased and active monomeric C subunits are released. PKA shares substrate specificity with Akt (PKB) and PKC, which are characterized by an arginine at position -3 relative to the phosphorylated serine or threonine residue (2). Substrates that present this consensus sequence and have been shown to be phosphorylated by PKA are Bad (Ser155), CREB (Ser133), and GSK-3 (GSK-3α Ser21 and GSK-3β Ser9) (3-5). In addition, combined knock-down of PKA C-α and -β blocks cAMP-mediated phosphorylation of Raf (Ser43 and Ser259) (6). Autophosphorylation and phosphorylation by PDK-1 are two known mechanisms responsible for phosphorylation of the C subunit at Thr197 (7).
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Montminy, M. (1997) Annu. Rev. Biochem. 66, 807-822.
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Dell'Acqua, M.L. and Scott, J.D. (1997) J. Biol. Chem. 272, 12881-12884.
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Tan, Y. et al. (2000) J. Biol. Chem. 275, 25865-25869.
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Gonzalez, G.A. and Montminy, M.R. (1989) Cell 59, 675-680.
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Fang, X. et al. (2000) Proc. Natl. Acad. Sci. USA 97, 11960-11965.
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Dumaz, N. and Marais, R. (2003) J. Biol. Chem. 278, 29819 -29823.
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Moore, M.J. et al. (2002) J. Biol. Chem. 277, 47878-47884.
