Analytical Data
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Gene name
VB2
- Application
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Alternative Names
VB2；Poxin
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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
Q01225
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Expression Region
1-219aa
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AA Sequence
MAMFYAHALGGYDENLHAFPGISSTVANDVRKYSVVSVYNNKYDIVKDKYMWCYSQVNKRYIGALLPMFECNEYLQIGDPIHDQEGNQISIITYRHKNYYALSGIGYESLDLCLEGVGIHHHVLETGNAVYGKVQHDYSTIKEKAKEMNALSPGPIIDYHVWIGDCICQVTAVDVHGKEIMRMRFKKGAVLPIPNLVKVKLGENDTENLSSTISAAPSR
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Molecular Weight
24.6 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 research on VB2 recombinant protein is rooted in its potential applications in various fields, including biotechnology and medicine. VB2, a viral protein derived from certain pathogens, has garnered interest due to its structural characteristics and ability to elicit immune responses. Understanding the protein's properties can lead to the development of effective vaccines and therapeutics. The recombinant expression of VB2 enables researchers to produce large quantities of the protein for detailed studies, including its interactions with host cells and its role in pathogenesis. Advances in genetic engineering techniques have facilitated the optimization of VB2 for better stability and bioactivity, paving the way for innovative diagnostic tools and treatments for viral infections. Furthermore, studying VB2's molecular mechanisms can enhance our understanding of viral evolution and inform strategies for combating emerging viruses. Overall, the investigation of VB2 recombinant protein holds promise for significant contributions to public health and disease management.
