Analytical Data
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Gene name
SEPX1
- Application
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Alternative Names
MSRB1;SEPX1;Methionine-R-sulfoxide reductase B1
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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
Q9NZV6
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Expression Region
1-116aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSFCSFFGGEVFQNHFEPGVYVCAKCGYEL FSSRSKYAHSSPWPAFTETIHADSVAKRPEHNRSEALKVSCGKCGNGLGH EFLNDGPKPGQSRFCIFSSSLKFVPKGKETSASQGH
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Molecular Weight
15 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
SEPX1, or Selenophosphate Synthetase 1, is a crucial enzyme that plays a significant role in the biosynthesis of selenoproteins, which are proteins that contain selenium, an essential micronutrient with antioxidant properties and vital physiological functions. Dysregulation of SEPX1 has been implicated in various diseases, including cancer and neurological disorders, due to its involvement in cellular redox balance and antioxidant defense mechanisms. Research on SEPX1 recombinant proteins focuses on elucidating its enzymatic function, understanding its role in selenoprotein synthesis, and exploring its potential as a therapeutic target. By producing recombinant SEPX1, scientists aim to study its biochemical properties in detail, including substrate specificity, catalytic mechanisms, and interactions with other cellular components. These studies can shed light on the broader implications of selenium in human health and disease, as well as the potential applications of selenoproteins in drug development and biotechnology. The investigation of SEPX1 and its recombinant forms may pave the way for innovative approaches to harness selenium's therapeutic benefits, contributing to advancements in dietary supplementation and disease intervention strategies.
