BAP31 (B-cell receptor-associated protein 31) is a transmembrane protein localized to the endoplasmic reticulum (ER), playing a critical role in ER protein quality control, vesicular trafficking, and apoptosis regulation. It interacts with various proteins, including caspase-8 and Bcl-2 family members, linking ER stress responses to apoptotic pathways. BAP31 antibodies are essential tools for studying its expression, localization, and molecular interactions in both physiological and pathological contexts.
These antibodies are widely used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to investigate BAP31's involvement in diseases such as cancer, neurodegenerative disorders, and immune dysregulation. For instance, in cancer research, BAP31 antibodies help elucidate its dual role as a pro-survival or pro-apoptotic factor, depending on cellular context and stress signals. In neurodegenerative studies, they aid in exploring connections between ER stress, protein misfolding, and neuronal death.
Commercial BAP31 antibodies are typically raised against specific epitopes, such as the N-terminal or C-terminal regions, with validation in human, mouse, or rat models. Researchers must verify antibody specificity using knockout controls due to potential cross-reactivity with homologous proteins like BAP29. Recent studies also utilize BAP31 antibodies to probe its post-translational modifications, including phosphorylation and ubiquitination, which regulate its functional switch between protein chaperoning and apoptosis signaling.