Analytical Data
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Gene name
vpr
- Application
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Alternative Names
vpr；KIAA0800；RIP；VPRBP；DDB1- and CUL4-associated factor 1
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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
O12160
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Expression Region
1-96aa
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AA Sequence
MEQAPEDQGPQREPYNEWTLELLEELKREAVRHFPRPWLHGLGQHIYETYGDTWTGVEAIIRILQRLLFVHFRIGCQHSRIGILRQRRARNGASRS
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Molecular Weight
18.9 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
Vpr (Viral protein R) is a unique accessory protein encoded by the human immunodeficiency virus type 1 (HIV-1) that plays critical roles in viral replication and pathogenesis. It is known to be involved in various cellular processes, including cell cycle regulation, apoptosis, and immune evasion, which are essential for the efficient replication of the virus. Research on Vpr has gained considerable attention due to its multifunctional nature and its potential as a target for therapeutic interventions against HIV. The protein is capable of interacting with host cellular factors, facilitating viral gene expression, and enhancing viral production. Additionally, Vpr has been implicated in promoting viral infectivity and the establishment of viral reservoirs in the host, complicating eradication efforts. The study of Vpr and its interactions at a molecular level is crucial for understanding the viral lifecycle and the mechanisms it employs to subvert host defenses. Moreover, the rational design of Vpr-based antiviral strategies could offer novel avenues for HIV treatment. Recent advances in recombinant protein technology have enabled researchers to produce Vpr in a laboratory setting, making it easier to investigate its structure-function relationships and to explore its role in HIV pathogenesis further. Overall, the ongoing research into Vpr is not only pertinent for understanding HIV biology but also for developing innovative therapeutic approaches to combat this global health challenge.
