Analytical Data
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Gene name
SELM
- Application
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Alternative Names
SELM；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
ATAYRPDWNRLSGLTRARVETCGGSQLNRLKEVKAFVTQDIPFYHNLVMK HLPGADPELVLLGRRYEELERIPLSEMTREEINALVQELGFYRKAAPDAQ VPPEYVWAPAKPPEETSDHADL
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Molecular Weight
14 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
SELM (Selenoprotein M) is a selenoprotein that plays a crucial role in various biological processes, including antioxidant defense, redox signaling, and modulation of cellular metabolism. Research has shown that SELM is involved in the regulation of selenium homeostasis and has implications in health and disease, particularly in relation to oxidative stress and inflammatory responses. Its unique selenium incorporation at specific cysteine residues allows SELM to exert its functions in protecting cells from oxidative damage. Altered expression of SELM has been linked to various pathological conditions, including cancer, neurodegenerative diseases, and cardiovascular disorders. Therefore, understanding the structure-function relationship and the molecular mechanisms underlying SELM’s actions is essential for elucidating its biological significance. Studying SELM in recombinant forms enables researchers to investigate its properties in detail, assess its interactions with other molecular partners, and explore its potential therapeutic applications. Moreover, SELM's role in selenium-dependent pathways highlights the importance of trace elements in human health, making it a focal point of research in nutritional biochemistry and disease prevention. As current findings pave the way for novel therapeutic strategies, the ongoing investigation of SELM continues to provide insights into its multifaceted roles in cellular physiology and its potential as a biomarker or target for therapeutic intervention in selenium-related diseases.
