protein

SULT1E1 Protein, Human (N-His)

HY-P76099A

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

72;115;300;480;1250;2000 USD

SULT1E1 Protein, Human (N-His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

72;115;300;480;1250;2000 USD

The SULT1E1 protein is a sulfotransferase that critically regulates estrogen homeostasis by sulfating estradiol and estrone, resulting in hormone inactivation. Its versatility extends to sulfated DHEA, pregnenolone, and xenobiotics such as ethinyl estradiol. SULT1E1 Protein, Human (N-His) is the recombinant human-derived SULT1E1 protein, expressed by E. coli , with N-His labeled tag.

Human

SULT1E1 protein, a sulfotransferase utilizing 3'-phospho-5'-adenylyl sulfate (PAPS) as a sulfonate donor, plays a pivotal role in estrogen homeostasis by catalyzing the sulfate conjugation of estradiol and estrone, contributing to the inactivation of these hormones. Beyond its primary function in estrogen metabolism, SULT1E1 demonstrates versatility by sulfating dehydroepiandrosterone (DHEA), pregnenolone, (24S)-hydroxycholesterol, and various xenobiotic compounds such as ethinylestradiol, equalenin, diethyl stilbesterol, and 1-naphthol, albeit with lower efficiency. Notably, SULT1E1 does not sulfonate cortisol, testosterone, and dopamine. Moreover, this sulfotransferase may be implicated in gut microbiota-host metabolic interactions, as it O-sulfonates 4-ethylphenol (4-EP), a tyrosine-derived metabolite produced by gut bacteria. The resulting product, 4-EPS, crosses the blood-brain barrier and potentially exerts regulatory effects on oligodendrocyte maturation and myelination, influencing the functional connectivity of brain regions associated with the limbic system. The diverse substrate specificity of SULT1E1 highlights its crucial role in hormonal regulation and suggests its involvement in broader physiological processes, including gut-brain interactions with potential implications for neurological functions.

Sulfotransferase 1E1; ST1E1; EST-1; Estrogen sulfotransferase; STE

Greater than 90% as determined by reducing SDS-PAGE

Lyophilized from a 0.22 μm filtered solution of 50 mM Tris-HCL, 200 mM NaCl, pH 7.4, 8% trehalose.

Room temperature in continental US; may vary elsewhere.