DAPK3 (Death-associated protein kinase 3), also known as ZIPK (Zipper-interacting protein kinase), is a serine/threonine kinase belonging to the death-associated protein kinase family. It plays a critical role in regulating apoptosis, autophagy, and cytoskeletal dynamics. Structurally, DAPK3 contains a kinase domain, a calmodulin-binding regulatory domain, and a nuclear localization signal, enabling its involvement in diverse cellular processes. Dysregulation of DAPK3 has been linked to cancer progression, neurodegenerative disorders, and cardiovascular diseases, highlighting its therapeutic potential.
DAPK3 antibodies are essential tools for studying the expression, localization, and functional roles of this kinase in biological and pathological contexts. These antibodies enable detection of endogenous DAPK3 via techniques like Western blotting, immunohistochemistry, and immunofluorescence. High-quality DAPK3 antibodies specifically recognize epitopes within conserved regions of the protein, aiding in distinguishing it from other DAPK family members. Research utilizing these antibodies has revealed DAPK3's tumor-suppressive functions in certain cancers, where its downregulation correlates with poor prognosis, while its pro-apoptotic activity in neurodegenerative models suggests neuroprotective mechanisms. Challenges in antibody development include ensuring cross-reactivity across species and minimizing non-specific binding. Continued refinement of DAPK3-targeting antibodies supports advancements in both mechanistic studies and drug discovery pipelines.