Analytical Data
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Gene name
vif
- Application
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Alternative Names
SOR protein
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Species
Human immunodeficiency
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Source
Yeast
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Tag
N- His-sumostar
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P69721
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Expression Region
1-192aa
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Molecular Weight
38.5 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
Vif (Virion Infectivity Factor) is a critical accessory protein encoded by the Human Immunodeficiency Virus (HIV) that plays a vital role in viral replication and infectivity. Initially, Vif was identified as a factor that counteracts the host's antiviral defense mechanisms, particularly the APOBEC3 family of cytidine deaminases, which exert potent anti-HIV activity by inducing hypermutation in viral genomes. The research on Vif and its recombinant protein has garnered substantial interest due to its functional significance in the HIV life cycle and its potential as a target for therapeutic intervention. Investigations have demonstrated that Vif’s ability to recruit cellular cofactors is essential for its function, shedding light on the intricate interactions between viral proteins and host factors. Moreover, the development of Vif recombinant proteins has facilitated studies on viral pathogenesis, host-pathogen interactions, and the exploration of novel antiviral strategies. Understanding the structural and functional attributes of Vif is imperative for designing effective HIV treatments and vaccines, making it a focal point in HIV research. The ongoing exploration of Vif’s mechanisms and its recombinant forms continues to provide valuable insights into the complex interplay of HIV with the immune system, paving the way for innovative therapeutic approaches against HIV/AIDS.
