Analytical Data
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Gene name
VPRBP
- Application
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Alternative Names
VPRBP；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
Q9Y4B6
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Expression Region
1045-1396aa
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AA Sequence
QAPINFTSRLNRRASFPKYGGVDGGCFDRHLIFSRFRPISVFREANEDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEASYNCHNSAITHLEPSRDGSLLLTSATWSQPLSALWGMKSVFDMKHSFTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLLTLFNPDLANNYKRNCATFNPTDDLVLNDGVLWDVRSAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHTVPALDQCRVVFNHTGTVMYGAMLQADDEDDLMEERMKSPFGSSFRTFNATDYKPIATIDVKRNIFDLCTDTKDCYLAVIENQGSMDALNMDTVCRLYEVGRQRLAE
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Molecular Weight
46.0 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
VPRBP, or Viral Protein R Binding Protein, is a crucial component in the study of viral pathogenesis and host interactions. It is primarily known for its association with the HIV-1 virus, where it plays a significant role in the viral life cycle by mediating the nuclear transport of viral proteins. Research on VPRBP has gained momentum due to its potential implications in understanding how viruses manipulate host cellular machinery for their replication and propagation. Investigating VPRBP allows researchers to explore the mechanisms through which viral proteins, particularly the HIV-1 Vpr protein, exploit host pathways to enhance infection efficiency and evasion of the immune response. Additionally, VPRBP's involvement in various cellular processes, such as apoptosis and cell cycle regulation, contributes to the broader understanding of tumor biology and viral-induced oncogenesis. By studying the structure, function, and interactions of VPRBP, scientists aim to identify new therapeutic targets for antiviral strategies and better comprehend the intricacies of viral-host dynamics. This research not only enhances our knowledge of viral biology but also has significant implications for developing innovative approaches in combating viral infections and associated diseases.
