Polo-like kinase 3 (PLK3), a member of the Polo-like kinase family, plays critical roles in cell cycle regulation, DNA damage response, and tumor suppression. It is involved in checkpoint control during G2/M transition, mitotic progression, and stress-induced pathways such as apoptosis and autophagy. PLK3 contains a conserved N-terminal kinase domain and a C-terminal Polo-box domain (PBD), which mediates substrate interactions and subcellular localization. Dysregulation of PLK3 has been linked to cancer, neurodegenerative diseases, and cardiovascular disorders, with its expression often downregulated in tumors, suggesting tumor-suppressive functions.
PLK3 antibodies are essential tools for studying its expression, localization, and activity in cellular contexts. These antibodies are commonly used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to detect endogenous PLK3 protein levels or post-translational modifications (e.g., phosphorylation). Specific monoclonal or polyclonal antibodies targeting distinct epitopes (e.g., kinase domain or PBD) enable researchers to investigate PLK3's interactions with substrates, such as p53 or CHK2. and its role in stress signaling pathways. Validated PLK3 antibodies are crucial for exploring its dual roles in promoting cell cycle arrest/apoptosis under stress and maintaining genomic stability, offering insights into therapeutic targeting in diseases like cancer.