The Phospho-PKC (Ser660) antibody is designed to detect protein kinase C (PKC) isoforms when phosphorylated at serine 660. a critical post-translational modification associated with PKC activation. PKC comprises a family of serine/threonine kinases that regulate diverse cellular processes, including proliferation, apoptosis, differentiation, and immune responses. Activation of PKC typically involves phosphorylation at conserved sites within the kinase domain (activation loop), turn motif, and hydrophobic motif. Ser660. located in the hydrophobic motif of certain PKC isoforms (e.g., PKC-βII), undergoes phosphorylation during maturation or in response to signaling cascades. This phosphorylation stabilizes the active conformation of PKC and is essential for its full enzymatic activity. The antibody is widely used in research to study PKC activation dynamics, particularly in pathways triggered by G protein-coupled receptors, growth factors, or oxidative stress. It has applications in Western blotting, immunofluorescence, and immunohistochemistry to assess PKC signaling in contexts such as cancer, diabetes, cardiovascular diseases, and neurological disorders. Dysregulated PKC activity, marked by aberrant phosphorylation, is implicated in tumor progression, insulin resistance, and inflammation, making this antibody a valuable tool for investigating disease mechanisms and therapeutic targets.