Dihydrolipoamide acetyltransferase (DLAT), a core component of the pyruvate dehydrogenase complex (PDC), plays a critical role in cellular energy metabolism by catalyzing the conversion of pyruvate to acetyl-CoA in mitochondria. Dysregulation of DLAT is implicated in metabolic disorders, neurodegenerative diseases, and cancer, making it a target for biomedical research. DLAT antibodies are immunological tools designed to detect and quantify DLAT protein expression, localization, and post-translational modifications in various experimental contexts. These antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to study mitochondrial function, metabolic reprogramming in cancer, or mechanisms underlying diseases like primary biliary cholangitis (PBC), where DLAT is an autoantigen. Commercial DLAT antibodies are typically raised against specific epitopes of human DLAT, with cross-reactivity validated in common model organisms like mice and rats. Rigorous validation using knockout controls or siRNA-mediated silencing ensures specificity. Recent studies also explore DLAT's role in the tumor microenvironment and its interaction with immune checkpoints, expanding the antibody's applications in immunotherapy research. Proper storage and optimization of antibody dilutions are essential to maintain reproducibility in experimental outcomes.