Analytical Data
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Gene name
SULT1A1
- Application
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Alternative Names
Aryl sulfotransferase Phenol sulfotransferase Phenol/aryl sulfotransferase
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Species
Mouse
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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
P52840
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Expression Region
1-291aa
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Molecular Weight
54 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.
Quality inspection process
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Protein Description
SULT1A1, or sulfotransferase 1A1, is an important enzyme involved in the sulfation process, which modifies various hormones, neurotransmitters, and xenobiotics, thereby playing a critical role in drug metabolism and detoxification. Research into SULT1A1 is crucial due to its implications in pharmacogenomics, as genetic polymorphisms in the SULT1A1 gene can influence individual responses to medications and the risk of adverse drug reactions. Moreover, SULT1A1 has been linked to various cancers, as its metabolic products can activate or deactivate carcinogenic compounds. The recombinant expression of SULT1A1 in heterologous systems, such as bacteria or yeast, has provided a valuable tool for studying its enzymatic properties, substrate specificity, and the effects of genetic variants on its activity. This research not only contributes to a better understanding of drug metabolism pathways but also aids in the development of therapeutic strategies aimed at modulating SULT1A1 activity for improved clinical outcomes. As such, the characterization of SULT1A1 through recombinant protein studies has emerged as a significant area of interest in both basic and applied biomedical research.
