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Human SULT2A1 / STD Protein (His Tag)

DHEA-ST,DHEAS,HST,hSTa,ST2,ST2A1,ST2A3,STD

Catalog Number P11411-H07E
Organism Species Human
Host E. coli
Synonyms DHEA-ST,DHEAS,HST,hSTa,ST2,ST2A1,ST2A3,STD
Molecular Weight The recombinant human SULT2A1consisting of 291 amino acids and migrates as an approximately 35 kDa band in SDS-PAGE under reducing conditions as predicted.
predicted N Met
SDS-PAGE
Purity > 97 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human SULT2A1 (NP_003158.2) (Ser 2-Glu 285) was expressed, with a polyhistide tag at the N-terminus.
Bio-activity
Research Area Signaling |Signal Transduction |Metabolism |Drug metabolism
Formulation Lyophilized from sterile 50mM Tris, 500mM NaCl, 20% glycerol, pH 8.0
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Hydroxysteroid sulfotransferase ( SULT2A1 ) is a key enzyme in the testicular and hepatic metabolism of 5alpha-androstenone, which is a major component of the off-odor and off-flavor in pork known as boar taint. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. SULT2A1 is a sulfo-conjugating phase II enzyme expressed at very high levels in the liver and intestine, the two major first-pass metabolic tissues, and in the steroidogenic adrenal tissue. SULT2A1 acts preferentially on the hydroxysteroids dehydroepiandrosterone, testosterone/dihydrotestosterone, and pregnenolone and on cholesterol-derived amphipathic sterol bile acids.
Reference
  • Chatterjee, B. 2005, Methods Enzymol. 400:165-91.
  • Liu,Y. et al., 2006, Chem Res Toxicol. 19 (11):1420-5.
  • Sinclair, PA. et al., 2006, J Mol Endocrinol  36 (2):301-11.
  • Yalcin, EB. et al., 2008, Drug Metab Lett  2 (3):198-204.