Analytical Data
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Gene name
SEPX1
- Application
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Alternative Names
MSRB1; SELR; SELX; SEP-X1; Methionine-R-Sulfoxide Reductase B1
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Species
Human
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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
Q9NZV6
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Expression Region
Met1~His116
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Molecular Weight
12kDa
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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
SEPX1 (Selenoprotein X 1) is a member of the selenoprotein family, which is characterized by the incorporation of selenium into its amino acid structure. This protein has garnered significant interest due to its crucial role in the redox regulation of cellular processes and its involvement in various physiological functions, including antioxidant defense and thyroid hormone metabolism. Dysregulation or mutations in the SEPX1 gene have been implicated in several health conditions, such as thyroid dysfunction and immune system disorders. The study of recombinant SEPX1 proteins is vital for understanding its biological functions and potential therapeutic applications. By producing SEPX1 in a recombinant form, researchers can delve into its structural properties, enzymatic activities, and interaction with other biomolecules. This research not only enhances our knowledge of selenoproteins as a whole but also aids in the development of novel strategies for treating diseases associated with selenium deficiency or selenoprotein dysfunction. Understanding SEPX1 better could pave the way for innovative interventions in conditions where selenium plays a pivotal role, underscoring the importance of exploring this protein within the broader context of health and disease.
