Analytical Data
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Gene name
Ba71V-107
- Application
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Alternative Names
Ba71V-107；
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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
Q89424
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Expression Region
1-117aa
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AA Sequence
MDTETSPLLSHNLSTREGIKQSTQGLLAHTIARYPGTTAILLGILILLVIILIIVAIVYYNRSVDCKSSMPKPPPSYYVQQPEPHHHFPVFFRKRKNSTSLQSHIPSDEQLAELAHS
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Molecular Weight
13.1 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
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Protein Description
Ba71V-107, a recombinant protein derived from the Ba71V strain of the vesicular stomatitis virus (VSV), has garnered significant attention in the field of virology and vaccine development. The Ba71V strain exhibits unique pathogenicity and immunogenic properties, making it a valuable model for studying viral behavior and host interactions. Research on Ba71V-107 focuses on its potential as a vaccine candidate due to its ability to elicit robust immune responses. This protein's structure and function have been characterized to investigate how it interacts with the host immune system, providing insights into the development of innovative therapeutic strategies against VSV and similar viruses. Additionally, Ba71V-107 has been explored for its applicability in oncolytic virotherapy, wherein engineered viruses selectively target and destroy cancer cells while sparing normal tissues. The study of Ba71V-107 not only contributes to advancements in viral research but also holds promise for the development of effective vaccines and treatments against various diseases, highlighting the need for ongoing research in this area.
