Analytical Data
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Gene name
SEPHS1
- Application
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Alternative Names
SEPHS1；SELD；SPS；SPS1；Selenide. water dikinase 1
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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
P49903
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Expression Region
1-392aa
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AA Sequence
STRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEAMMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPETSGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS
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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 (Selenophosphate Synthetase 1) is an enzyme critical for selenoprotein synthesis, playing a pivotal role in the incorporation of selenium into these proteins. Selenoproteins are essential for various biological processes, including antioxidant defense, redox regulation, and thyroid hormone metabolism. The study of SEPHS1 is particularly significant because selenium is a trace element necessary for human health, and its deficiency has been linked to several diseases, such as Keshan disease and certain cancers. Research on SEPHS1 involves elucidating its structure-function relationship, regulation within the cellular environment, and its interactions with other cellular components to understand better how selenium metabolism impacts health. Recent advancements in recombinant protein technology have facilitated the production of SEPHS1, enabling further investigations into its enzymatic mechanisms and potential therapeutic applications. Understanding the intricate workings of SEPHS1 and its role in selenoprotein biosynthesis can provide insights essential for developing strategies to combat selenium deficiency-related diseases and harnessing the therapeutic potential of selenoproteins in health and disease.
