Analytical Data
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Gene name
VP30
- Application
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Alternative Names
(Minor nucleoprotein VP30)
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Species
strain Musoke-80
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35258
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Expression Region
1-281aa
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Molecular Weight
39.1 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
Related Products
Protein Description
VP30 is a key protein in the lifecycle of Ebola virus (EBOV), a member of the Filoviridae family and responsible for severe hemorrhagic fever in humans and other primates. The study of VP30 is crucial for understanding the mechanisms of Ebola virus pathogenesis and immune evasion. VP30 is known to play a significant role in the transcriptional activity of the viral genome, functioning as a transcription factor that is essential for the production of viral mRNA. Research indicates that VP30 can influence the formation of viral nucleoprotein complexes and regulate the viral life cycle, making it a potential target for therapeutic intervention. Given the lack of approved vaccines and treatments for Ebola, elucidating the structure and function of VP30 can provide insights into viral replication processes and highlight strategies for antiviral drug development. Furthermore, studies on VP30 can enhance our understanding of other emerging viral threats and contribute to global health security by identifying novel approaches for vaccine design and therapeutic strategies against filoviruses. As the global community faces the challenge of responding to viral outbreaks, thorough investigations into the functional dynamics of VP30 not only advance virology but also pave the way for innovative solutions to combat future infectious disease emergencies. Overall, research on VP30 is integral to developing effective countermeasures against Ebola virus and mitigating its impact on public health.
