Analytical Data
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Gene name
SULT1C2
- Application
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Alternative Names
SULT1C2；SULT1C2；Sulfotransferase 1C4
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00338
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Expression Region
1-296aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMALTSDLGKQIKLKEVEGTLLQPATVDNWS QIQSFEAKPDDLLICTYPKAGTTWIQEIVDMIEQNGDVEKCQRAIIQHRH PFIEWARPPQPSGVEKAKAMPSPRILKTHLSTQLLPPSFWENNCKFLYVA RNAKDCMVSYYHFQRMNHMLPDPGTWEEYFETFINGKVVWGSWFDHVKGW WEMKDRHQILFLFYEDIKRDPKHEIRKVMQFMGKKVDETVLDKIVQETSF EKMKENPMTNRSTVSKSILDQSISSFMRKGTVGDWKNHFTVAQNERFDEI YRRKMEGTSINFCMEL
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Molecular Weight
37 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
Related Products
Protein Description
SULT1C2, a member of the sulfotransferase enzyme family, plays a crucial role in the biotransformation of various endogenous and exogenous compounds, including hormones, neurotransmitters, and drugs. This enzyme catalyzes the sulfate conjugation process, which significantly influences the pharmacokinetics and pharmacodynamics of numerous substances by altering their solubility, bioactivity, and excretion rates. Research on SULT1C2 has gained prominence due to its potential implications in drug metabolism and personalized medicine, as genetic variations in sulfotransferases can lead to diverse therapeutic responses among individuals. Additionally, SULT1C2 is implicated in the metabolism of environmental chemicals and toxins, making it a focal point in toxicological studies. The recombinant production of SULT1C2 allows for detailed biochemical characterization, providing insights into its substrate specificity, kinetic properties, and potential regulatory mechanisms. Understanding SULT1C2's functional dynamics is essential for elucidating its role in health and disease, as well as for developing strategies to modulate its activity in therapeutic settings. Overall, the study of SULT1C2 recombinant proteins is significant for advancing our comprehension of sulfation processes and enhancing drug design and safety assessments.
