Ca, cAMP & Lipid Signaling
- Ca, cAMP & Lipid Signaling
PhosphoSitePlus®：
PKACa
- 推奨プロトコール
PKA C-α Antibody |
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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8日17時20分 現在 |
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| #4782S | 100 μL | 46,000 | 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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4782 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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| ウェスタンブロッティング (1:1,000)、免疫沈降 (1:50)、免疫蛍光細胞染色(IF-IC) (1:100)、フローサイトメトリー (1:50) |
| 種交差性 | |
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| ヒト、マウス、ラット |
| 特異性・感度 | |
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| 内在性レベルのPKA C-αタンパク質を検出します。 |
| 検出タンパク質の分子量 | |
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| 42 kDa |
| 使用抗原 | |
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| ヒトのPKA C-αタンパク質のC末端配列 (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
Western blot analysis of extracts from HeLa, C6, PC12 and NIH/3T3 cells, using PKA C-α Antibody.
Western Blotting
Western blot analysis of extracts from HeLa cells transfected with non-targeted (-) or PKA C-α (+) siRNA. PKA C-α was detected using the PKA C-α Antibody #4782, and Akt1 was detected using Akt1 (2H10) Monoclonal Antibody #2967. The PKA C-α Antibody confirms silencing of PKA C-α expression, and the Akt1 Antibody is used to control for loading and specificity of PKA C-α siRNA.
Western Blotting
Western blot analysis of extracts from HeLa cells, transfected with either 100 nM SignalSilence® Control siRNA (Fluorescein Conjugate) #6201 (-), SignalSilence® PKA C-α siRNA II (+) or SignalSilence® PKA C-α siRNA I #6406 (+), using PKA C-α Antibody #4782 and α-Tubulin (11H10) Rabbit mAb #2125. The PKA C-α antibody confirms silencing of PKA C-α expression and α-Tubulin (11H10) Rabbit mAb is used to control for loading and specificity of PKA C-α siRNA.
Flow Cytometry
Flow cytometric analysis of HeLa cells, using PKA C-α Antibody (blue) compared to a nonspecific negative control antibody (red).
IF-IC
Confocal immunofluorescent analysis of HeLa cells using PKA C-alpha Antibody (green). Actin filaments have been labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5™ (fluorescent DNA dye).
| バックグラウンド |
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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).
- Montminy, M. (1997) Annu. Rev. Biochem. 66, 807-822.
- Dell'Acqua, M.L. and Scott, J.D. (1997) J. Biol. Chem. 272, 12881-12884.
- Tan, Y. et al. (2000) J. Biol. Chem. 275, 25865-25869.
- Gonzalez, G.A. and Montminy, M.R. (1989) Cell 59, 675-680.
- Fang, X. et al. (2000) Proc. Natl. Acad. Sci. USA 97, 11960-11965.
- Dumaz, N. and Marais, R. (2003) J. Biol. Chem. 278, 29819 -29823.
- Moore, M.J. et al. (2002) J. Biol. Chem. 277, 47878-47884.
| 使用例 | |
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本製品は試験研究用です。