Analytical Data
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Gene name
X27S,X28S,X29S
- Application
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Alternative Names
(Ag35)(Virion envelope protein p35)(Fragments)
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Species
Vaccinia virus
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Source
E. coli
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P30895
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Expression Region
1-56aa(X27S,X28S,X29S)
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Molecular Weight
7.5 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
The recombinant proteins X27S, X28S, and X29S are part of an ongoing investigation into the functional and structural properties of proteins derived from specific organisms. These proteins are of interest due to their potential applications in biotechnology and medicine, including their roles in molecular interactions and enzymatic activities. Each variant, differentiated by minor sequence changes, may exhibit unique characteristics that can influence their stability, activity, or interaction with other biomolecules. Research on these proteins focuses on understanding the mechanisms underlying their functions, exploring their potential as therapeutic agents, and leveraging their properties for industrial applications. By employing techniques such as protein expression, purification, and characterization, scientists aim to elucidate the biological relevance and practical utility of X27S, X28S, and X29S. This work contributes to a broader understanding of protein engineering and opens avenues for innovations in drug development and synthetic biology.
