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The Protein Kinase C (PKC) family of homologous serine/threonine protein kinases is involved in a number of processes, such as growth, differentiation, and cytokine secretion. 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 the 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 members. The C-terminal region of PKC contains the catalytic domain. The PKC pathway represents a major signal transduction system that is activated following ligand-stimulation of transmembrane receptors by hormones, neurotransmitters, and growth factors. PKCθ transcripts are expressed in most tissues with the highest levels being found in hematopoietic tissues and cell lines, including T cells and thymocytes. PKCθ mRNA is readily detectable in skeletal muscle, lung and brain. However, PKCθ expression is not detected in several human carcinoma cell lines. Abundant expression of this PKC isozyme in hematopoietic cells suggest that it may have a role in growth and differentiation processes of these cells.Host Species: MouseClone: 27Isotype: IgG2a κSpecies Reactivity: HumanImmunogen: Human PKCθ aa. 21-217Formula Weight [Chemical]: 79kDaImmunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
