- SynonymSULT1B1,ST1B1,ST1B2,SULT1B2,Sulfotransferase 1B2
- SourceHuman SULT1B1 (2-296), His Tag (SU1-H5148) is expressed from E.coli cells. It contains AA Leu 2 - Ile 296 (Accession # AAH10895).Predicted N-terminus: MetRequest for sequence
- Molecular Characterization
This protein carries a polyhistidine tag at the N-terminus.
The protein has a calculated MW of 35.8 kDa. The protein migrates as 35.8 kDa under reducing (R) condition (SDS-PAGE).
- EndotoxinLess than 1.0 EU per μg by the LAL method.
- Purity
>95% as determined by SDS-PAGE.
- Formulation
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH 7.5. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
- Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
- Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human SULT1B1 (2-296), His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
- BackgroundSulfotransferase family cytosolic 1B member 1 (SULT1B1) is also known as sulfotransferase 1B2 (ST1B2) and thyroid hormone sulfotransferase, which is an enzyme that in humans is encoded by the SULT1B1 gene. 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. Furthermore, sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites.
- References
- (1)Dombrovski L., et al., 2006, Proteins 64:1091-1094.
- (2)Wang J., et al., 1998, Mol. Pharmacol. 53:274-282.
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