PKCβ Mouse, Unlabeled, Clone: 36, BD

Description

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. 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. PKCβ is highly expressed in brain and hematopoietic cells. Autophosphorylation of PKCβ occurs at the N- and C-terminal regions, as well as within the hinge region. However, only the COOH- terminal autophosphorylation sites are essential for PKCβ's function and subcellular localization. PKCβ is critical for the proliferation of K562 cells, as well as being an important regulator of human melanogenesis.

Host Species: Mouse
Clone: 36
Isotype: IgG2a
Species Reactivity: Rat
Immunogen: Human PKCβ aa. 126-324
Formula Weight [Chemical]: 80kDa

Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting