Analytical Data
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Gene name
SULT1B1
- Application
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Alternative Names
SULT1B1；ST1B2；Sulfotransferase 1B1
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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
O43704
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Expression Region
1-296aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLSPKD ILRKDLKLVH GYPMTCAFAS NWEKIEQFHS RPDDIVIATY PKSGTTWVSE IIDMILNDGD IEKCKRGFIT EKVPMLEMTL PGLRTSGIEQ LEKNPSPRIV KTHLPTDLLP KSFWENNCKM IYLARNAKDV SVSYYHFDLM NNLQPFPGTW EEYLEKFLTG KVAYGSWFTH VKNWWKKKEE HPILFLYYED MKENPKEEIK KIIRFLEKNL NDEILDRIIH HTSFEVMKDN PLVNYTHLPT TVMDHSKSPF MRKGTAGDWK NYFTVAQNEK FDAIYETEMS KTALQFRTEI
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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
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Protein Description
SULT1B1, a member of the sulfotransferase family, plays a crucial role in the phase II metabolism of various endogenous and exogenous compounds by catalyzing the sulfonation process. This enzyme is particularly significant in the detoxification of drugs, hormones, and neurotransmitters, influencing their bioavailability and pharmacological activity. Research into SULT1B1 has garnered attention due to its implications in drug metabolism and the potential development of personalized medicine approaches. Notably, variations in SULT1B1 expression and activity have been associated with differences in individual responses to medications, adverse drug reactions, and susceptibility to certain diseases. Understanding the structure and function of SULT1B1 through recombinant protein studies can illuminate its catalytic mechanisms and offer insights into its regulatory pathways. Furthermore, the generation of SULT1B1 recombinant protein facilitates the development of assay systems for screening drug candidates, exploring enzyme inhibitors, and advancing the study of disease associations. Overall, SULT1B1 represents a promising target for further research to enhance drug efficacy and safety profiles in clinical settings.
