Analytical Data
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Gene name
SEPN1
- Application
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Alternative Names
RSS; MDRS1; RSMD1; SELN; SEP-N1; Rigid Spine Muscular Dystrophy 1
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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
Q9NZV5
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Expression Region
Leu79~His291
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Molecular Weight
30kDa
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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
SEPN1 (Selenoprotein N) is a crucial protein encoded by the SEPN1 gene, primarily recognized for its role in human muscle function and oxidative stress response. Mutations in the SEPN1 gene are linked to various muscle disorders, particularly a rare myopathy known as SEPN1-related myopathy, which manifests as muscle weakness, respiratory issues, and contractures. The protein contains a selenocysteine residue incorporated into its structure, emphasizing its importance in selenium metabolism and antioxidant defense mechanisms. Research on SEPN1 recombinant proteins aims to elucidate their biological functions and structure, enabling a better understanding of the molecular mechanisms underlying SEPN1-related diseases. The production of SEPN1 as a recombinant protein facilitates the study of its biochemical properties and offers potential avenues for therapeutic interventions. Moreover, insights gained from these studies may pave the way for the development of biomarkers for early diagnosis and targeted treatments of muscle disorders associated with SEPN1 deficiencies. The increasing interest in redox biology and mitochondrial function further highlights the significance of SEPN1 in health and disease, underscoring the importance of ongoing research in this field.
