The USP15 antibody is a crucial tool for studying ubiquitin-specific protease 15 (USP15), a deubiquitinating enzyme belonging to the ubiquitin-specific protease (USP) family. USP15 regulates protein stability and signaling pathways by removing ubiquitin chains from target substrates, thereby modulating processes like protein degradation, DNA repair, immune response, and cellular homeostasis. It interacts with diverse substrates, including TGF-β receptors, IKKγ/NEMO, and parkin, implicating it in cancer, neurodegenerative diseases (e.g., Parkinson’s), and inflammatory disorders. Researchers use USP15 antibodies in techniques such as Western blotting, immunoprecipitation, and immunofluorescence to detect USP15 expression, localization, and activity in cells or tissues. These antibodies are often validated for specificity using knockout cell lines or siRNA-mediated silencing to ensure accurate target recognition. USP15’s dual role as an oncogene or tumor suppressor, depending on context, makes its antibody valuable for exploring context-dependent regulatory mechanisms. Additionally, USP15 antibodies aid in studying post-translational modifications, substrate interactions, and therapeutic targeting, such as evaluating small-molecule inhibitors for cancer treatment. Its involvement in critical pathways underscores the antibody’s importance in both basic research and translational applications.