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Phospho-PKC (pan) (zeta Thr410) (190D10) Rabbit mAb
synthetic phosphopeptide corresponding to residues surrounding Thr410 of human PKC zeta
W
详见说明书
H,M,R,Mk
大量
详见MSDS文件
CST
1
-20°c
100 ul (10 western blots)/300 ul (30 western blots)/carrier free & custom formulation / quantity
规格: | 产品价格: | ¥请询价 | |
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规格: | 100 ul (10 western blots) | 产品价格: | ¥请询价 |
规格: | 300 ul (30 western blots) | 产品价格: | ¥请询价 |
规格: | carrier free & custom formulation / quantity | 产品价格: | ¥请询价 |
pathway more info application references datasheet PDF MSDS PDF protocols
Applications Key: W=Western Blotting
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Applications | Reactivity | Sensitivity | MW (kDa) | Isotype |
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W | H M R Mk | Endogenous | 76 to 85 | Rabbit IgG |
Protocols |
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Specificity / Sensitivity | Phospho-PKC (pan) (zeta Thr410) (190D10) Rabbit mAb detects endogenous levels of PKC alpha, beta I, beta II, gamma, delta, epsilon, eta, theta and iota isoforms only when phosphorylated at a residue homologous to threonine 410 of human PKCzeta. |
Source / Purification | Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr410 of human PKC zeta. |
Background | 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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Application References |
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Companion Products |
Rabbit Monoclonals Produced Using Epitomics® Technology, U.S. Patent No. 5,675,063. For Research Use Only. Not For Use In Diagnostic Procedures. |
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