Estrogen sulfotransferase, also known as Sulfotransferase, estrogen-preferring, Sulfotransferase 1E1, SULT1E1 and ST1E1, is a cytoplasm enzyme which belongs to the sulfotransferase 1 family. 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. SULT1E1 may control the level of the estrogen receptor by sulfurylating free estradiol. SULT1E1 maximally sulfates beta-estradiol and estrone at concentrations of 20 nM. SULT1E1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, equalenin, diethylstilbesterol and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated. SULT1E1 is a key enzyme in estrogen homeostasis. It plays a central role in the prevention and development of human disease.
Recombinant Human SULT1E1/ST1E1 Protein (His Tag)
£585.60 – £732.00 excluding VAT
Size | 50µg |
---|---|
Active Protein | |
Activity | |
Protein Construction | A DNA sequence encoding the human SULT1E1 (NP_005411.1) (Asn 2-Ile 294) was expressed, with a polyhistidine tag at the N-terminus. |
Sequence | Asn 2-Ile 294 |
Fusion Tag | N-His |
Accession | NP_005411.1 |
Species | Human |
Expressed Host | E.coli |
Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
Purity | > 92 % as determined by reducing SDS-PAGE. |
Endotoxin | Please contact us for more information. |
Stability and Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
Mol Mass | 36 kDa |
AP Mol Mass | 33 kDa |
Formulation | Lyophilized from sterile 20mM Tris 0.5M NaCl, 20% glycerol, pH 8.0 |
Research Areas | Signal Transduction, metabolism |
Reconstitution | Please refer to the printed manual for detailed information. |