Protein Kinase D2 (PKD2), a serine/threonine kinase belonging to the PKD family, plays critical roles in cellular signaling pathways regulating proliferation, migration, apoptosis, and vesicle trafficking. It is activated by diacylglycerol (DAG) and protein kinase C (PKC) isoforms, influencing downstream targets like HDACs, SLAM, and β-catenin. PKD2 is widely expressed in tissues, including the heart, pancreas, and immune cells, with distinct roles in organ-specific physiology and pathology.
Antibodies targeting PKD2 are essential tools for studying its expression, localization, and function. These antibodies, often raised in rabbits or mice, enable techniques such as Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF). Specific epitopes or phosphorylation sites (e.g., Ser876/Ser878) are targeted to assess activation status. Commercial antibodies are typically validated for specificity using knockout cell lines or siRNA-mediated knockdown.
Research using PKD2 antibodies has linked the kinase to diseases like cancer, cardiovascular disorders, and immune dysregulation. For example, PKD2 overexpression is implicated in prostate and breast cancer progression, while its suppression affects cardiac hypertrophy. Additionally, PKD2 modulates T-cell receptor signaling and insulin secretion in pancreatic β-cells, highlighting therapeutic potential. Challenges remain in distinguishing cross-reactivity with PKD1/PKD3 due to structural homology, necessitating careful antibody validation. Overall, PKD2 antibodies are vital for unraveling its multifaceted roles in health and disease.