SULT2B1 (sulfotransferase family 2B member 1) is a cytosolic enzyme that catalyzes the sulfonation of steroids, cholesterol, and other hydroxysteroids, modulating their solubility, bioactivity, and metabolic fate. It exists as two splice variants, SULT2B1a and SULT2B1b, differing in substrate specificity and tissue distribution. SULT2B1b, the predominant isoform, is highly expressed in the prostate, placenta, and skin, where it sulfonates cholesterol and oxysterols, influencing lipid homeostasis and signaling pathways.
Antibodies targeting SULT2B1 are critical tools for studying its expression, localization, and functional roles in physiological and pathological contexts. They are widely used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence to investigate tissue-specific expression patterns or dysregulation in diseases such as prostate cancer, psoriasis, and hormone-dependent disorders. Many commercially available SULT2B1 antibodies are raised against specific peptide sequences unique to the SULT2B1 isoforms, enabling selective detection. Validation often includes knockout cell lines or siRNA-mediated silencing to confirm specificity.
Research utilizing these antibodies has highlighted SULT2B1's involvement in cholesterol sulfate production (critical for skin barrier integrity) and its potential role in cancer progression via steroid metabolism. However, cross-reactivity with other sulfotransferases remains a technical consideration, emphasizing the need for rigorous antibody validation in experimental settings.