Sulfotransferase 1A2, ST1A2, Aryl sulfotransferase 2, Phenol sulfotransferase 2, Phenol-sulfating phenol sulfotransferase 2, P-PST 2, SULT1A2, STP2, HAST4, TSPST2.
SULT1A2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-295 a.a.) and having a molecular mass of 36.4kDa.
SULT1A2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Sulfotransferase 1A2, ST1A2, Aryl sulfotransferase 2, Phenol sulfotransferase 2, Phenol-sulfating phenol sulfotransferase 2, P-PST 2, SULT1A2, STP2, HAST4, TSPST2.
MGSSHHHHHH SSGLVPRGSH MELIQDISRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG TTWVSQILDM IYQGGDLEKC HRAPIFMRVP FLEFKVPGIP SGMETLKNTP APRLLKTHLP LALLPQTLLD QKVKVVYVAR NAKDVAVSYY HFYHMAKVYP HPGTWESFLE KFMAGEVSYG SWYQHVQEWW ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETV DLMVEHTSFK EMKKNPMTNY TTVRREFMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL.
The Sulfotransferase Family, Cytosolic, 1A, Member 2 (SULT1A2) is a protein-coding gene that belongs to the sulfotransferase family. These enzymes play a crucial role in the sulfate conjugation of various hormones, neurotransmitters, drugs, and xenobiotic compounds. The SULT1A2 gene encodes one of the phenol sulfotransferases with thermostable enzyme activity .
SULT1A2 utilizes 3’-phospho-5’-adenylyl sulfate (PAPS) as a sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs, and neurotransmitters. This enzyme is also responsible for the sulfonation and activation of minoxidil, a drug used for hair growth. Additionally, SULT1A2 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA-binding products, potentially modulating cancer risk .
Human recombinant SULT1A2 is used in various research and industrial applications to study its role in drug metabolism, hormone regulation, and potential implications in cancer research. The recombinant form allows for controlled studies and the development of assays to measure enzyme activity and substrate specificity .