Recombinant Human SULT2A1 protein

SULT2A1 (sulfotransferase family 2A member 1) is a cytosolic enzyme belonging to the sulfotransferase superfamily, which plays a critical role in phase II drug metabolism and the regulation of endogenous compounds. This enzyme catalyzes the transfer of a sulfonate group from the cofactor 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to hydroxyl or amine groups of various substrates, enhancing their water solubility and facilitating excretion. SULT2A1 is primarily expressed in the liver, adrenal glands, and intestines, with a particular focus on detoxifying xenobiotics (e.g., drugs, environmental toxins) and modulating bioactive endogenous molecules such as steroids, bile acids, and neurosteroids.

Recombinant SULT2A1 protein is produced through genetic engineering techniques, typically by expressing the human SULT2A1 gene in heterologous systems like Escherichia coli or mammalian cell lines. This allows large-scale production of the purified enzyme for functional studies, structural analysis, and drug development applications. Researchers utilize recombinant SULT2A1 to investigate substrate specificity, enzyme kinetics, and inhibitory mechanisms, which are essential for understanding drug-drug interactions and individual variations in drug metabolism. Its role in steroid sulfation also links it to endocrine regulation, cancer progression (e.g., hormone-sensitive tumors), and metabolic disorders. However, challenges remain in maintaining the enzyme's stability and PAPS cofactor dependency during in vitro assays. Current studies focus on optimizing recombinant SULT2A1 production and exploring its therapeutic potential in targeting sulfation pathways implicated in diseases like cholestasis, hormone-dependent cancers, and neuropsychiatric conditions.