DAP Kinase 1 (DAPK1) is a calcium/calmodulin-regulated serine/threonine kinase that plays a critical role in apoptosis, autophagy, and membrane blebbing. Initially identified for its pro-apoptotic function in interferon-γ-induced cell death, DAPK1 is implicated in tumor suppression, neurodegenerative diseases, and immune regulation. Structurally, it contains a kinase domain, a calmodulin-binding regulatory segment, a cytoskeleton-binding domain, and a death domain, enabling interactions with diverse signaling molecules. Dysregulation of DAPK1. often through epigenetic silencing (e.g., promoter hypermethylation in cancers), is linked to uncontrolled cell proliferation, metastasis, and chemoresistance. In Alzheimer’s and stroke, its overactivation contributes to neuronal death.
Antibodies targeting DAPK1 are essential tools for studying its expression, localization, and post-translational modifications (e.g., autophosphorylation at Ser308/311 for activity regulation). They are widely used in Western blotting, immunohistochemistry, and immunofluorescence to assess DAPK1 levels in cancer tissues, neurological models, or cell lines under stress conditions. Some antibodies specifically detect phosphorylated forms to evaluate kinase activation status. Commercial DAPK1 antibodies are typically raised against epitopes in the N-terminal kinase domain or C-terminal regions, with validation in knockout controls to ensure specificity. Their applications extend to biomarker discovery, therapeutic targeting studies, and elucidating DAPK1's dual roles in cell survival and death pathways.