Analytical Data
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Gene name
Selenot
- Application
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Alternative Names
Selenot；SELT；Thioredoxin reductase-like selenoProtein T
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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
P62341
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Expression Region
20-195aa
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AA Sequence
S ANLGGVPSKR LKMQYATGPL LKFQICVSUG YRRVFEEYMR VISQRYPDIR IEGENYLPQP IYRHIASFLS VFKLVLIGLI IVGKDPFAFF GMQAPSIWQW GQENKVYACM MVFFLSNMIE NQCMSTGAFE ITLNDVPVWS KLESGHLPSM QQLVQILDNE MKLNVHMDSI PHHRS
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Molecular Weight
22.3 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
Selenoproteins are a unique class of proteins that contain selenium in the form of the amino acid selenocysteine. One significant member of this family is Selenot, which is implicated in various biological processes, including antioxidant defense, thyroid hormone metabolism, and cellular redox regulation. Research into Selenot and its recombinant protein form has garnered attention due to its potential roles in human health and disease. Notably, selenoproteins are essential for proper immune function and may play a protective role against oxidative stress, which has been linked to conditions such as cancer and cardiovascular diseases. The recombinant expression of Selenot allows for the exploration of its structural and functional properties, facilitating studies on its role in cellular mechanisms. Moreover, understanding Selenot not only enhances our knowledge of selenoprotein biology but also opens avenues for therapeutic applications, as manipulation of its expression and activity could lead to novel strategies for disease prevention and treatment. As such, ongoing research is focused on elucidating the biochemical pathways involving Selenot, the mechanisms of its action, and how alterations in its expression may contribute to various health conditions. This research is pivotal in advancing our comprehension of selenium's contributions to health, informing dietary recommendations, and potentially leading to innovative clinical interventions.
