Analytical Data
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Gene name
Selenot
- Application
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Alternative Names
Selenot; Selt; Thioredoxin reductase-like selenoprotein T; SelT; EC 1.8.1.9
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Species
Mouse
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P62342
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Expression Region
20-195aa
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Molecular Weight
24.2 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
Selenot, a selenium-binding protein, has garnered significant attention in the field of biochemistry and molecular biology due to its unique role in selenium metabolism and potential implications for human health. Selenium is an essential trace element with antioxidant properties, and its bioavailability is closely linked to various biological functions, including immune response and inflammatory processes. Research has shown that Selenot may act as a critical player in the incorporation of selenium into selenoproteins, which are vital for cellular protection against oxidative stress and regulation of redox balance. Given the rising interest in the therapeutic potential of selenoproteins, studies focusing on the recombinant expression and characterization of Selenot hold promise for understanding its structure-function relationships and elucidating its mechanistic roles within the cell. Furthermore, insights gained from Selenot research could lead to novel strategies for disease prevention and treatment, particularly in conditions associated with selenium deficiency or dysregulation. Overall, the investigation of recombinant Selenot serves as a vital stepping stone in comprehensively unraveling the complex biochemistry of selenium and its essential contributions to health.
