SULT2A1 (sulfotransferase family 2A member 1) is a Phase II conjugating enzyme that catalyzes the sulfonation of steroids, bile acids, and xenobiotics using 3'-phosphoadenosine-5'-phosphosulfate (PAPS) as the sulfate donor 1. The enzyme mediates sulfation of hydroxysteroids including DHEA, testosterone, pregnenolone, and bile acids, with bile acid 3-sulfation being catalyzed exclusively by SULT2A1 12. Sulfonation generally increases water solubility and renal excretion, though can occasionally result in bioactivation of xenobiotics 3. SULT2A1 expression is transcriptionally regulated by multiple nuclear receptors including vitamin D receptor, farnesoid X receptor, pregnane X receptor, and retinoid-related orphan receptors 12. The enzyme requires direct physical interaction with PAPSS2 for efficient DHEA sulfation, explaining why PAPSS2 mutations manifest with undetectable DHEA sulfate and androgen excess 4. Clinically, SULT2A1 polymorphisms influence nevirapine metabolism and associated adverse reactions 3, while SULT2A1 deficiency in hepatocellular carcinoma promotes stemness and chemotherapy resistance through AKT pathway activation 5. Reduced SULT2A1 expression in liver diseases including steatohepatitis, fibrosis, and hepatocellular carcinoma correlates with impaired ROR expression 2.