**Background of Phospho-PKCδ (Y311) Antibody**
The Phospho-PKCδ (Y311) antibody is designed to detect protein kinase C delta (PKCδ) when phosphorylated at tyrosine residue 311. PKCδ, a member of the novel PKC subfamily, is a serine/threonine kinase involved in diverse cellular processes, including apoptosis, proliferation, differentiation, and stress responses. Its activity is tightly regulated by post-translational modifications, such as phosphorylation. Phosphorylation at Y311. located in the catalytic domain, is critical for modulating PKCδ’s enzymatic activity, substrate specificity, and subcellular localization.
This phosphorylation event is often linked to oxidative stress, DNA damage, or activation of tyrosine kinase receptors (e.g., EGFR, Src). Studies suggest that Y311 phosphorylation enhances PKCδ’s pro-apoptotic functions, particularly in contexts like cancer, neurodegeneration, and cardiovascular diseases. For instance, in response to genotoxic stress, phosphorylated PKCδ (Y311) translocates to the nucleus, promoting cell cycle arrest or apoptosis by interacting with substrates such as p73 or DNA repair proteins.
The Phospho-PKCδ (Y311) antibody is widely used in research to investigate PKCδ activation dynamics in signaling pathways and disease models. Specificity for the phosphorylated Y311 epitope enables precise detection in techniques like Western blotting, immunofluorescence, or immunohistochemistry. Understanding PKCδ regulation via Y311 phosphorylation provides insights into therapeutic targeting of PKCδ-associated pathologies, including chemoresistance in cancers or ischemic injury.