The protein kinase C epsilon (PRKCE or PKCε) antibody is a crucial tool for studying the epsilon isoform of the protein kinase C (PKC) family, a group of serine/threonine kinases involved in diverse cellular signaling pathways. PKCε belongs to the novel PKC subfamily, which requires diacylglycerol (DAG) or phorbol esters for activation but does not depend on calcium. Structurally, it contains a regulatory domain with tandem C1 motifs for lipid binding and a catalytic domain for phosphorylation. PKCε plays roles in cell proliferation, survival, migration, and stress responses, with implications in cancer, cardiac diseases, and neurological disorders. Dysregulation of PKCε is linked to tumor progression, chemoresistance, ischemic preconditioning in the heart, and neuroinflammation.
PRKCE antibodies are used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to detect PKCε expression, localization, and activation status. Specificity is critical, as PKC isoforms share structural homology; rigorous validation via knockout controls or siRNA knockdown ensures minimal cross-reactivity. Researchers employ these antibodies to explore PKCε's involvement in signaling pathways (e.g., NF-κB, MAPK) and its interactions with downstream targets. In drug discovery, they help assess therapeutic agents targeting PKCε in diseases like cancer or heart failure. Overall, PRKCE antibodies are indispensable for unraveling the kinase's pathophysiological roles and translational potential.