Analytical Data
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Gene name
SULT1A4
- Application
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Alternative Names
Sulfotransferase 1A4. ST1A4. EC:2.8.2.1. Aryl sulfotransferase 1A3/1A4. Sulfotransferase 1A3/1A4
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0DMN0
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Expression Region
1-295 aa
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AA Sequence
MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
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Molecular Weight
32.5 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
SULT1A4, a member of the sulfotransferase family, is involved in the sulfation of various substrates, including drugs, hormones, and neurotransmitters. This enzyme plays a critical role in the Phase II metabolism of xenobiotics, facilitating their excretion and reducing potential toxicity. Research on SULT1A4 has gained momentum due to its implications in pharmacogenomics, where genetic variations can influence drug metabolism and therapeutic responses. This is particularly relevant in personalized medicine, where understanding an individual's metabolic capacity can optimize treatment regimens. Moreover, SULT1A4 has been implicated in the metabolism of compounds associated with certain diseases, suggesting a broader physiological relevance. The recombinant expression of SULT1A4 provides a valuable tool for exploring its activity, substrate specificity, and interactions with various chemicals. By producing large quantities of the enzyme, researchers can conduct kinetic studies and investigate the enzyme's role in drug interactions and side effects. Additionally, recombinant SULT1A4 can aid in the discovery of novel inhibitors or activators, contributing to the development of better therapeutic strategies. Overall, the study of SULT1A4 recombinant protein is vital for advancing our understanding of sulfation processes and their impact on drug efficacy and safety.
