Analytical Data
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Gene name
VACWR156
- Application
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Alternative Names
VACWR156; A33RProtein A33
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Species
Vaccinia virus
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P68617
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Expression Region
57-185aa
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Molecular Weight
16.2 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
VACWR156 is a recombinant protein derived from the Vaccinia virus, which has garnered attention due to its potential applications in immunology and virology. The Vaccinia virus, known for its use in the smallpox vaccine, possesses various proteins that promote immune evasion; VACWR156 is one such protein believed to play a crucial role in modulating host immune responses. Research into VACWR156 focuses on understanding its mechanism of action in suppressing the host's antiviral immunity and its potential to enhance vaccine efficacy. By elucidating the biochemical pathways and interactions mediated by VACWR156, scientists aim to develop targeted therapies that could mimic or counteract its immune-modulating effects. This could lead to innovative vaccine strategies and treatments for viral infections, particularly in the context of emerging pathogens. Additionally, investigating the role of VACWR156 has broader implications for biotechnological applications, such as using its properties for improving recombinant vaccine designs. The ongoing exploration of VACWR156 underscores the importance of studying viral proteins not only to comprehend their roles in pathogen survival but also to leverage this knowledge for advancing public health strategies.
