Ca, cAMP & Lipid Signaling
- Ca, cAMP & Lipid Signaling
PhosphoSitePlus®：
PKCZ
- 推奨プロトコール
PKCζ Antibody |
イイネ！(0) | 
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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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| #9372S | 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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9372 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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下記ステップについては、データシートの右側もあわせてご参照ください。
IHC-P: 抗体希釈液 / 抗原賦活化
| 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)、免疫組織染色 (パラフィン) (1:50) |
| 種交差性 | |
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| ヒト |
| 特異性・感度 | |
|---|---|
| 内在性レベルのPKCζタンパク質を検出します。内在性レベルの他のPKC アイソフォームとは交差しません。 |
| 検出タンパク質の分子量 | |
|---|---|
| 78 kDa |
| 使用抗原 | |
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| ヒトのPKCζタンパク質 (合成ペプチド) |
| 抗体の由来 | |
|---|---|
| ウサギ |
| 貯法 | |
|---|---|
| -20℃ |
| 社内データ |
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Western Blotting
Western blot analysis of Baculovirus expressed PKC isoforms, demonstrating the isoform-specificty of PKCζ Antibody.
Western Blotting
Western blot analysis of extracts of HeLa, 293, THP1 and PL45 cells, using PKCζ Antibody.
IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human renal cell carcinoma, using PKCζ Antibody.
IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human lung carcinoma, showing nuclear and cytoplasmic localization using PKCζ Antibody.
IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human ovarian adenocarcinoma, using PKCζ Antibody.
IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human lung carcinoma, using PKCζ Antibody in the presence of control peptide (left) or antigen specific peptide (right).
| バックグラウンド |
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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).
- Nishizuka, Y. (1984) Nature 308, 693-698.
- Keranen, L.M. et al. (1995) Curr. Biol. 5, 1394-1403.
- Mellor, H. and Parker, P.J. (1998) Biochem J. 332 (Pt 2), 281-292.
- Ron, D. and Kazanietz, M.G. (1999) FASEB J. 13, 1658-1676.
- Moscat, J. and Diaz-Meco, M.T. (2000) EMBO Rep. 1, 399-403.
- Baron, C.L. and Malhotra, V. (2002) Science 295, 325-328.
- Flynn, P. et al. (2000) J. Biol. Chem. 275, 11064-11070.
- Kawagoe, T. et al. (2008) Nat Immunol 9, 684-91.
| 使用例 | |
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| 製品をご使用いただいて研究を発表されましたら、ぜひお知らせください。 |
本製品は試験研究用です。