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| Product Name | Protein Kinase C Inhibitor, zeta, Pseudosubstrate, Myristoylated |
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| Description | Purity ~90% by HPLC and MS analysis. Activation of PKC is one of the earliest events in the cascade leading to a variety of cellular responses such as secretion, gene expression, proliferation and muscle contraction. PKC isoforms have been classified in three groups: classical PKCs, which are Ca2+ dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG) and phorbol esters (TPA or PMA) through their cysteine-rich C1 domains; novel PKCs, which are Ca2+ independent but are still regulated by PS, DAG and TPA; and atypical PKCs, which are Ca2+ independent and do not require PS, DAG or TPA for their activation. These three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to the substrate binding site in the catalytic domain preventing its activation in the absence of cofactors or activators. Other members have been recently added to the PKC superfamily based on homology within the catalytic domain. PKCmu, or PKD, is regulated |
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| Size | 1mg |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | n/a |
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| Gene, Accession, CAS # | n/a |
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| Catalog # | P9103-71 |
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| Order / More Info | Protein Kinase C Inhibitor, zeta, Pseudosubstrate, Myristoylated from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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