Analytical Data
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Gene name
sei
- Application
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Alternative Names
sei；SEI1；TRIPBR1；SERTA domain-containing Protein 1
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Species
E.coli
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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
A0A0H3JSY8
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Expression Region
1-242aa
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AA Sequence
MKKFKYSFILVFILLFNIKDLTYAQGDIGVGNLRNFYTKHDYIDLKGVTDKNLPIANQLEFSTGTNDLISESNNWDEISKFKGKKLDIFGIDYNGPCKSKYMYGGATLSGQYLNSARKIPINLWVNGKHKTISTDKIATNKKLVTAQEIDVKLRRYLQEEYNIYGHNNTGKGKEYGYKSKFYSGFNNGKVLFHLNNEKSFSYDLFYTGDGLPVSFLKIYEDNKIIESEKFHLDVEISYVDSN
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Molecular Weight
43.9 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
SEI (Selenocysteine Incorporation Factors) is a class of proteins of significant interest in the field of molecular biology and biochemistry due to their unique role in facilitating the incorporation of selenocysteine, the 21st amino acid, into proteins during translation. Selenocysteine is crucial for various biological processes, particularly in antioxidant defense and redox regulation, as it is a component of several essential selenoproteins. Research on SEI proteins has gained momentum as scientists seek to understand their mechanisms of action, interactions with ribosomes, and their regulatory roles in selenoprotein synthesis. The importance of selenoproteins in human health and disease, including their implications in cancer, neurodegenerative diseases, and immunity, underscores the relevance of SEI protein studies. Furthermore, understanding the molecular frameworks governing selenocysteine incorporation could pave the way for novel therapeutic strategies and biotechnological applications, such as the design of engineered proteins with enhanced functional properties. Consequently, the exploration of SEI proteins offers a promising avenue for advancing our understanding of protein synthesis and function, with potential implications for health and disease management.
