Analytical Data
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Gene name
SULT1A2
- Application
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Alternative Names
SULT1A2;STP2;Sulfotransferase 1A2
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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
P50226
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Expression Region
1-295aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMELIQDISRPPLEYVKGVPLIKYFAEALGP LQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVP FLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLDQKVKVVYVAR NAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWW ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFK EMKKNPMTNYTTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADY AEKMAGCSLSFRSEL
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Molecular Weight
36 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
SULT1A2, or Sulfotransferase 1A2, is a member of the sulfontransferase family, which plays a crucial role in the metabolism of various endogenous compounds, xenobiotics, and drugs through the process of sulfonation. This enzyme is particularly important in the detoxification and bioactivation of numerous pharmacological agents and environmental toxins. Research into SULT1A2 is motivated by its potential implications in drug metabolism, cancer biology, and various metabolic disorders. Moreover, variations in the expression and activity of SULT1A2 can significantly influence individual responses to medications, making it a key target for pharmacogenomic studies. The recombinant protein expression of SULT1A2 allows for detailed functional studies, characterization of substrate specificity, and investigation of the enzyme's role in metabolic pathways. Understanding the structure and function of SULT1A2 provides insights into its regulatory mechanisms and interaction with various substrates, which is vital for developing personalized medicine approaches and improving therapeutic outcomes. Additionally, exploring the enzyme's role in physiological and pathological processes can contribute to identifying new therapeutic targets for diseases associated with dysregulated metabolism.











