PKCalpha (Central region) (clone M237), anti-human, mouse, rat

Background:
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. PKC consists of a single polypeptide chain containing four conserved regions (C) and five variable regions (V). The N-terminal half interacts with PKC activators Ca2+, phospholipid, diacylglycerol, or phorbol ester, while the C-terminal half contains the catalytic domain. The conventional PKC subfamily (alpha, beta I, beta II, and gamma) is regulated by both Ca2+ and diacylglycerol. The PKC pathway represents a major signal transduction system that is activated following ligand-stimulation of transmembrane receptors by hormones, neurotransmitters, and growth factors. The phosphorylation of multiple sites in conventional PKCs regulates their activity. In mast cells, FceRI stimulation leads to phosphorylation of tyrosine 658 and 662 of PKCbeta I and PKCalpha, respectively. This phosphorylation requires autophosphorylation of serine 657 and 661 in these respective kinases.

Immunogen: Clone (M237) was generated from a recombinant human PKCα that included amino acids residues in the central region. This region is highly conserved in rat and mouse PKCα, and has homology to conserved regions in PKCβ.

Specificity: This antibody detects an 82kDa* protein corresponding to the molecular mass of PKCα on SDS-PAGE immunoblots of neonatal rat brain and adult mouse brain lysates.

Buffer/Storage:
Mouse monoclonal antibody purified with protein A chromatography is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.