Analytical Data
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Gene name
SEPHS1
- Application
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Alternative Names
Selenium donor protein 1 Selenophosphate synthase 1
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P49903
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Expression Region
1-392aa
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Molecular Weight
69.8 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
SEPHS1, or selenophosphate synthetase 1, is a critical enzyme involved in the biosynthesis of selenoproteins, which are proteins that contain the rare element selenium. These proteins play vital roles in various biological processes, including antioxidant defense, redox regulation, and thyroid hormone metabolism. The proper function of SEPHS1 is essential for maintaining selenium homeostasis in cells and organisms. Research on SEPHS1 has gained attention due to its implications in human health and disease, particularly in conditions such as cancer, cardiovascular disease, and neurodegenerative disorders. Abnormalities in selenoprotein synthesis, linked to dysfunctional SEPHS1 activity, have been associated with increased oxidative stress and inflammation. Studies have aimed to better understand the enzyme's structure, function, and regulation, as well as its interaction with other metabolic pathways involving selenium and antioxidant mechanisms. Moreover, the development of recombinant SEPHS1 proteins can facilitate detailed biochemical assays and screening for potential inhibitors or modulators, contributing to therapeutic strategies against diseases linked to selenium imbalances. As researchers continue to explore the molecular intricacies of SEPHS1, its potential as a biomarker for selenium nutrition and as a therapeutic target in selenium-related pathologies is becoming increasingly evident, paving the way for future advancements in nutritional sciences and medicine.
