The protein kinase C mu (PKCμ), also known as protein kinase D1 (PKD1), is a serine/threonine kinase belonging to the PKD family, initially classified as an atypical PKC due to structural similarities. Unlike classical PKC isoforms, PKCμ/PKD1 contains a pleckstrin homology (PH) domain and a cysteine-rich motif, enabling its role in membrane trafficking, cell survival, and signal transduction. It is activated by diacylglycerol (DAG) and phosphorylation via PKC isoforms, responding to stimuli like oxidative stress, G protein-coupled receptors (GPCRs), and growth factors.
PKCμ antibodies are essential tools for studying its expression, localization, and activation in diseases, particularly cancer. Overexpression of PKCμ is linked to tumor progression, metastasis, and resistance to therapy in cancers such as prostate, breast, and pancreatic malignancies. These antibodies enable detection of total PKCμ or its phosphorylated forms (e.g., at Ser744/748 or Ser916), reflecting activation status. Applications include Western blotting, immunohistochemistry, and immunofluorescence, aiding research on PKCμ's role in cellular processes like apoptosis, angiogenesis, and immune regulation. Commercial PKCμ antibodies are typically validated for specificity using knockout controls or siRNA-based approaches. Ongoing studies explore PKCμ as a therapeutic target, with inhibitors under investigation for oncologic applications.