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- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
The Protein Kinase C (PKC) family of homologous serine/threonine protein kinases. At least eleven isozymes have been described. These proteins are products of multiple genes and alternative splicing. PKC consists of a single polypeptide chain containing four conserved regions (C) and five variable regions (V). The N-terminal half containing C1, C2, V1, and V2 constitutes the regulatory domain and interacts with PKC activators Ca2+, phospholipid, diacylglycerol, or phorbol ester. However, the novel PKC (nPKC) subfamily members (δ, ε, η, and θ isoforms) and the atypical PKC (aPKC) subfamily members (ζ, ι, and λ isoforms) are Ca2+ independent and lack the C2 domain. The aPKC members are unique in that their activity is independent of diacylglycerols and phorbol esters. They also lack one repeat of the cysteine-rich sequences that are conserved in cPKC and nPKC. The C-terminal region of PKC contains the catalytic domain. PKCδ is involved in myeloid differentiation, as well as in the secretory response of antigen-stimulated rat basophilic RBL 2H3 cells. Overexpression and subsequent stimulation of PKCδ leads to cell cycle arrest in CHO cells and complete growth inhibition of NIH 3T3 cells. PKCδ is the most abundant isoform in hemopoietic cells and is highly expressed in many other organs and tissues. This suggests that PKCδ may be one of the major PKC isozymes in mammalian cells.
研发参考 (5)
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Bell RM, Burns DJ. Lipid activation of protein kinase C. J Biol Chem. 1991; 266(8):4661-4664. (Biology). 查看参考
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Blass M, Kronfeld I, Kazimirsky G, Blumberg PM, Brodie C. Tyrosine phosphorylation of protein kinase Cdelta is essential for its apoptotic effect in response to etoposide. Mol Cell Biol. 2002; 22(1):182-195. (Clone-specific: Immunofluorescence, Immunoprecipitation, Western blot). 查看参考
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Larsen EC, Ueyama T, Brannock PM, et al. A role for PKC-epsilon in Fc gammaR-mediated phagocytosis by RAW 264.7 cells. J Cell Biol. 2002; 159(6):939-944. (Clone-specific: Immunofluorescence, Western blot). 查看参考
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Nishizuka Y. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature. 1988; 334(6184):661-665. (Biology). 查看参考
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Ringshausen I, Schneller F, Bogner C, et al. Constitutively activated phosphatidylinositol-3 kinase (PI-3K) is involved in the defect of apoptosis in B-CLL: association with protein kinase Cdelta. Blood. 2002; 100(10):3741-3748. (Clone-specific: Immunoprecipitation). 查看参考
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