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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 PKC activators Ca2), phospholipid, diacylglycerol, or phorbol ester. However, the novel PKC (nPKC) subfamily members (δ, η, η, and θ isoforms) and the atypical PKC (aPKC) subfamily members (ζ , ι , and λ isoforms) are Ca(2 ) independent and lack the C2 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. Expression of the 90kDa PKCα is induced by interferon-α. Generally, PKCα is expressed at very low levels in normal murine tissues, except brain. Overexpression of PKCα leads to increased growth rates and higher cell densities in monolayer cultures. A high level of expression is seen in several hematopoietic cell lines and tumors. This suggests a possible role for PKCα in tumorigenesis.Host Species: MouseClone: 21Isotype: IgG2aSpecies Reactivity: RatImmunogen: Human PKCε aa. 1-175Formula Weight [Chemical]: 90kDaImmunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
