Analytical Data
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Gene name
SELM
- Application
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Alternative Names
SELENOM; SELM; Selenoprotein M; SelM
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Species
Human
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Source
E. coli
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Tag
Tag Free
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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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Molecular Weight
13.9 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 (Sel1-like repeat-containing protein) is a crucial protein involved in various cellular processes, including protein homeostasis and quality control within the endoplasmic reticulum. Research into SELM recombination has gained momentum due to its potential implications in understanding diseases associated with protein misfolding and aggregation, such as neurodegenerative disorders. SELM is known for its role in the unfolded protein response (UPR), a cellular mechanism that is activated in response to stressors, allowing cells to manage excessive misfolded proteins. Emerging studies suggest that SELM may interact with various molecular chaperones and assist in the folding of nascent polypeptides, thus playing a vital role in maintaining cellular function. Investigating the recombinant forms of SELM can provide insights into its structural dynamics and functional mechanisms, potentially leading to the development of therapeutic strategies targeting protein misfolding diseases. Furthermore, SELM's involvement in cellular signaling pathways highlights its significance in cancer biology and other pathophysiological conditions. Understanding the intricacies of SELM's interaction with other cellular constituents may aid in delineating the pathways that contribute to disease progression, thereby underscoring the importance of SELM in both basic and applied biomedical research.
