Analytical Data
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Gene name
SELENOM
- Application
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Alternative Names
SELENOM；SELM；SelenoProtein M
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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
Q8WWX9
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Expression Region
24-145aa
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AA Sequence
ATAYRPDWNRLSGLTRARVETCGGSQLNRLKEVKAFVTQDIPFYHNLVMKHLPGADPELVLLGRRYEELERIPLSEMTREEINALVQELGFYRKAAPDAQVPPEYVWAPAKPPEETSDHADL
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Molecular Weight
13.9kDa
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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
SELENOM, or selenocysteine-containing proteins, are crucial components in various biological processes due to their unique properties conferred by the incorporation of selenium in the form of selenocysteine. This amino acid plays a pivotal role in antioxidant defense, redox regulation, and thyroid hormone metabolism, contributing to the maintenance of cellular homeostasis and protection against oxidative stress. Research into SELENOM recombinant proteins focuses on their functional characterization, mechanisms of action, and potential therapeutic applications. The ability to produce these proteins through recombinant DNA technology allows for a better understanding of their structure-function relationships and the exploration of their roles in diseases linked to selenium imbalances, such as cancer and cardiovascular conditions. Given the rising interest in nutritional selenium and its implications for health, studying SELENOM offers valuable insights that could lead to novel biomolecular strategies in disease prevention and treatment.
