Ca, cAMP & Lipid Signaling
Phospho-PKCα/β II (Thr638/641) Antibody
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| CSTコード |
包装 |
希望納入価格 (円) |
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| #9375S | 100 μL | 57,000 | |
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| #9375P | 40 μL for Custom Sampler Kit |  Custom Antibody Sampler Kitの構成品を選択できます。
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シグナル伝達研究応援キャンペーン プレゼント *Pサイズのみ
PKC抗体製品一覧
9375 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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9375:
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Immunoprecipitation
Western Blotting
| 用途(希釈倍率) | |
| ウエスタンブロッティング(1:1,000)、免疫沈降(1:100) |
| 特異性・感度 | |
| Thr638 がリン酸化されたPKC α タンパク質およびThr641 がリン酸化されたPKC βⅡ タンパク質を検出します。PKCβⅠおよびγタンパク質とも弱くですが交差します。 |
| 検出タンパク質の分子量 | |
| 80 kDa、82 kDa |
| 使用抗原 | |
| ヒトのPKC α タンパク質のThr638 周辺領域(合成ペプチド) |
| ※括弧付きの動物種は配列が100%相同であるため反応すると推定されます。 |
Western Blotting

Western blot analysis of Baculovirus-expressed PKC isoforms alpha, beta, gamma, delta and epsilon, untreated or treated with lambda protein phosphatase, using Phospho-PKCalpha/beta II (Thr638/641) Antibody (upper) or PKCalpha, beta, gamma, delta, epsilon antibodies (lower).
Western Blotting

Western blot analysis of extracts from 293 cells, untreated, TPA treated (200 nM), or treated with TPA and CIP and λ phosphatases using Phospho-PKCα/βII (Thr638/641) Antibody or PKCα Antibody #2056.
Sequence

Phosphorylation of PKCalpha
Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation at Thr500 in the activation loop, the autophosphorylation site at Thr641, and at carboxy-terminal hydrophobic site Ser660 occurs in vivo (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. Either the enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).
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Nishizuka, Y. (1984) Nature 308, 693-698.
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Keranen, L.M. et al. (1995) Curr. Biol. 5, 1394-1403.
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Mellor, H. and Parker, P.J. (1998) Biochem J. 332 (Pt 2), 281-292.
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Ron, D. and Kazanietz, M.G. (1999) FASEB J. 13, 1658-1676.
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Moscat, J. and Diaz-Meco, M.T. (2000) EMBO Rep. 1, 399-403.
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Baron, C.L. and Malhotra, V. (2002) Science 295, 325-328.
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Flynn, P. et al. (2000) J. Biol. Chem. 275, 11064-11070.