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Overview
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Recombinant Human SULT1E1 produced in E. Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-294 a.a.) and having a molecular mass of 36.1 kDa. SULT1E1 is fused to 6 amino acid His Tag at C-terminus and purified by conventional chromatography techniques. SULT1E1 catalyzes the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. SULTIE1 control the level of the estrogen receptor by sulfurylating free estradiol. maximally sulfates beta-estradiol and estrone at concentrations of 20nm. SULTIE1 in addition sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, equalenin, diethylstilbesterol and 1-naphthol, at considerably higher concentrations; though, cortisol, testosterone and dopamine are not sulfated. Decreased SULT1E1 expression is linked with estrogen-dependent endometrial carcinomas. Altered cellular proliferation was detected in cells stably expressing SULT1E1.
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Overview