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#2058 PKCδ Antibody

CSTコード 包装
希望納入価格 (円)
国内在庫 i
2020年2月26日16時0分 現在
ご登録代理店情報 i
#2058S100 μL58,000


感度分子量 (kDa)抗体の由来貯法
種交差性 (社内試験済)
交差する可能性がある種 i


ヒト、マウス、ラット、サル -
2058 の推奨プロトコール i

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。



ウェスタンブロッティング (1:1000)免疫沈降 (1:25)


内在性レベルのPKCδタンパク質を検出します。内在性レベルの他のPKC タンパク質のアイソフォームとは交差しません。
ヒトのPKCδタンパク質 (合成ペプチド)

ホモロジー (相同性) 検索をご希望の場合 >>>



※下記の社内データは、すべて2058 の推奨プロトコールで実験した結果です。

Western Blotting

Western Blotting

Western blot analysis of Baculovirus expressed PKC isoforms, demonstrating the isoform-specificity of PKCδ Antibody.

Western Blotting

Western Blotting

Western blot analysis of extracts of HeLa, COS, C6 and NIH/3T3 cells, using PKCδ Antibody.


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 occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (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. 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).

Phosphorylatioin of tyrosine residues in PKCdelta are suggested to play a role in determining its functional properties. Phosphorylated tyrosine residues have been identified in the catalytic domain, regulatory domain, and the hinge of PKCdelta (8). While no clear designation of regulatory specificity has been deciphered based on phosphorylated tyrosine patterns, these various phosphorylations have been shown to decrease PKCdelta protein level, increase kinase activity or increase selectivity of substrate specificity (8-10).

12630   SignalFire™ Plus ECL Reagent
12757   SignalFire™ Elite ECL Reagent
14787   Phospho-PKCδ (Ser359) (D2X1P) Rabbit mAb
2051   Phospho-PKD/PKCμ (Ser916) Antibody
2054   Phospho-PKD/PKCμ (Ser744/748) Antibody
2055   Phospho-PKCdelta (Tyr311) Antibody
2056   PKCα Antibody
2261   Phospho-(Ser) PKC Substrate Antibody
6883   SignalFire™ ECL Reagent
7074   Anti-rabbit IgG, HRP-linked Antibody
7727   Biotinylated Protein Ladder Detection Pack
93292   Phospho-PKCδ (Thr505) (D8K4R) Rabbit mAb
9371   Phospho-PKC (pan) (βII Ser660) Antibody
9372   PKCζ Antibody
9374   Phospho-PKCδ (Thr505) Antibody
9375   Phospho-PKCα/β II (Thr638/641) Antibody
9376   Phospho-PKCδ/θ (Ser643/676) Antibody
9377   Phospho-PKCθ (Thr538) Antibody
9378   Phospho-PKCζ/λ (Thr410/403) Antibody
9379   Phospho-PKC (pan) (gamma Thr514) Antibody
9921   Phospho-PKC Antibody Sampler Kit
9960   PKC Isoform Antibody Sampler Kit

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PKCδ Antibody

Immune Cell Signaling Pathways