ANTI-PROTEIN KINASE C

Anti-Protein Kinase C α has been used in immunoblotting and immunohistochemistry.

Protein Kinase C (PKC) is a phospholipid and calcium dependent enzyme that regulates intracellular signal transduction. Neuronal PKC modulates several functions such as nerve cell excitability, neuronal plasticity, and release of neurotransmitters. PKC inhibitors have been implicated in diabetic retinopathy . Monoclonal Anti-Protein Kinase C (clone MC5) recognizes an epitope located within the amino acid sequence 296-317 at the hinge region (close to or at the trypsin cleavage site) of PKC . The antibody is specific for PKC in humans, bovines, rats and mice. Binding of the antibody to in vitro purified PKC blocks trypsin-mediated partial proteolysis. Phorbol-ester induced down-regulation of the kinase is inhibited by the introduction of Fab fragment of the antibody into a rodent glioma cell line .

Protein Kinase C (PKC) plays a crucial role in signal transduction leading to cellular regulation, cell growth and differentiation, oncogenesis and modulation of neurotransmission. PKC is a phospholipid dependent enzyme, activated by the lipid 1,2-diacylglycerol (DAG), an intracellular second messenger produced as a result from hydrolysis of inositol phospholipids, in response to a variety of hormones, growth factors and neurotransmitters. PKC is also the major cellular receptor for the tumor promoting phorbol esters. PKC action is mediated by binding to specific receptors for activated C-kinase (RACKs) and through the phosphorylation of several cellular substrates. Overexpression and stimulation of PKC α leads to enhanced growth rate of cells in culture. Anti-Protein Kinase C α antibody is useful for studying expression of PKC α in normal and neoplastic tissues.