Ca, cAMP & Lipid Signaling
PKCε (22B10) Rabbit mAb
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| CSTコード |
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| #2683S | 100 μL | 46,000 | |
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PKCepsilon抗体製品一覧
2683 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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2683:
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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PKCεタンパク質を検出します。他のPKC アイソフォームとは交差しません。 |
| 使用抗原 | |
| ヒトのPKCεタンパク質由来の配列 (合成ペプチド) |
Western Blotting
Western blot analysis of extracts from mouse brain, PC12 and COS cells using PKCε (22B10) Rabbit mAb.
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.
PhosphoSitePlus®：
PKCE