Analytical Data
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Gene name
VP35
- Application
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Alternative Names
VP35；MEM3；Vacuolar Protein sorting-associated Protein 35
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Species
Human
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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
Q6V1Q9
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Expression Region
1-340aa
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AA Sequence
MTTRTKGRGHTAATTQNDRMPGPELSGWISEQLMTGRIPVSDIFCDIENNPGLCYASQMQQTKPNPKTRNSQTQTDPICNHSFEEVVQTLASLATVVQQQTIASESLEQRITSLENGLKPVYDMAKTISSLNRVCAEMVAKYDLLVMTTGRATATAAATEAYWAEHGQPPPGPSLYEESAIRGKIESRDETVPQSVREAFNNLDSTTSLTEENFGKPDISAKDLRNIMYDHLPGFGTAFHQLVQVICKLGKDSNSLDIIHAEFQASLAEGDSPQCALIQITKRVPIFQDAAPPVIHIRSRGDIPRACQKSLRPVPPSPKIDRGWVCVFQLQDGKTLGLKI
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Molecular Weight
42.4kDa
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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
VP35 protein, an essential component of the Ebola virus, plays a crucial role in viral replication and immune evasion. As a non-structural protein, VP35 acts primarily as a viral polymerase cofactor, facilitating the transcription and replication of the viral genome. Its ability to inhibit interferon (IFN) signaling is of particular interest, as it allows the virus to evade the host’s innate immune response. Research has shown that VP35 interferes with the host cell’s immune system by disrupting the function of various pattern recognition receptors and by blocking the activation of transcription factors necessary for IFN production. Given the high mortality rate associated with Ebola virus infections and the lack of approved antiviral therapies, understanding the molecular mechanisms of VP35 is critical for developing effective treatments and vaccines. Recent studies have focused on the structure-function relationship of VP35, exploring its potential as a target for drug design and therapeutic intervention. Additionally, advancements in recombinant protein expression systems have enabled the production of VP35 for further functional studies and screening assays, thereby enhancing our understanding of its role in the viral life cycle and informing strategies for combating Ebola virus disease. Overall, research on VP35 represents a significant step toward unraveling the complexities of Ebola virus pathogenesis and contributes to the broader field of viral immunology.
