Anti-Human SULT1A1 Antibody Pair

Product Description: Sulfotransferase family 1A member 1 (SULT1A1) is a cytosolic phase II enzyme that catalyzes the transfer of a sulfate group from the cofactor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to hydroxyl and amine groups of various substrates, including hormones, neurotransmitters, drugs, and xenobiotics. Structurally, SULT1A1 features a single alpha/beta domain with a central five-stranded parallel beta-sheet and a dynamic active-site cap that regulates substrate access. Key loops (L1, L2, L3) form a gating mechanism controlling substrate binding, with phenylalanine residues (F81, F84) acting as a molecular clamp to enhance substrate affinity and catalysis. The enzyme exhibits tissue-dependent substrate specificity influenced by PAPS occupancy and harbors two allosteric sites that modulate activity. Functionally, SULT1A1 plays a major role in hepatic detoxification and metabolism. Variations in SULT1A1 activity and expression are linked to altered drug metabolism and susceptibility to cancers, such as breast and lung cancer, and influence responses to environmental toxins and carcinogens. Protein Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine group. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important role in the sulfonation of endogenous molecules such as steroid hormones (PubMed:12471039, PubMed:16221673, PubMed:21723874, PubMed:22069470, PubMed:7834621). Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil (By similarity). Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (PubMed:7834621). May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system (PubMed:35165440). Catalyzes the sulfate conjugation of dopamine (PubMed:8093002). Catalyzes the sulfation of T4 (L-thyroxine/3,5,3',5'-tetraiodothyronine), T3 (3,5,3'-triiodothyronine), rT3 (3,3',5'-triiodothyronine) and 3,3'-T2 (3,3'-diiodothyronine), with a substrate preference of 3,3'-T2 > rT3 > T3 > T4 (PubMed:10199779) [The Uniprot Consortium]