Phospho-PRKCA (S657/Y658) Polyclonal Antibody

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 (α, β1, βII, and γ) 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 PKCα and PKCβI respectively. This phosphorylation requires autophosphorylation of serine 657 and 661 in these respective kinases.

This antibody detects an 82kDa* protein corresponding to the molecular mass of phosphorylated PKCα on SDS-PAGE immunoblots of neonatal rat brain lysate. Similar results were observed in human SKN-SH, endothelial, and HeLa cells, as well as rabbit spleen fibroblasts and rat pituitary cells.