Analytical Data
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Gene name
SULT1B1
- Application
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Alternative Names
DOPA/tyrosine sulfotransferase
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Species
Rat
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P52847
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Expression Region
1-299aa
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Molecular Weight
54.8 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
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Protein Description
SULT1B1, a member of the sulfotransferase family, plays a crucial role in the biotransformation of various endogenous and exogenous compounds by catalyzing the sulfate conjugation process. This enzyme is particularly important in the metabolism of hormones, neurotransmitters, and drugs, thereby influencing their bioactivity and elimination from the body. Research has shown that SULT1B1 is involved in the regulation of the pharmacokinetics and pharmacodynamics of numerous therapeutic agents, which can impact drug efficacy and toxicity. Recent studies have highlighted the significance of SULT1B1 in various physiological and pathological contexts, including its potential role in cancer progression and drug resistance. The recombinant expression of SULT1B1 protein allows for detailed investigations into its enzymatic activity, substrate specificity, and potential as a biomarker for therapeutic responses. Furthermore, understanding SULT1B1's genetic variations among populations could help tailor personalized medicine approaches. As a result, the study of SULT1B1 recombinant protein holds promise not only for advancing our knowledge of drug metabolism but also for developing novel therapeutic strategies in the field of pharmacology and toxicology.
