Cat: PA2000-3760

Recombinant Human vif Protein,His

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Analytical Data

  • Gene name

    vif

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    vif;Virion infectivity factor

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P69721

  • Expression Region

    1-192aa

  • AA Sequence

    MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH

  • Molecular Weight

    38.5 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

Vif (Virion Infectivity Factor) is a key protein produced by the Human Immunodeficiency Virus (HIV) that plays a crucial role in counteracting the antiviral activity of host cellular factors, specifically a class of proteins known as APOBECs (Apolipoprotein B mRNA Editing Enzyme Catalytic Polypeptides). APOBECs can edit the viral DNA during reverse transcription, leading to the incorporation of mutations that severely impair viral replication. However, Vif helps HIV evade this restriction by targeting APOBECs for degradation through the ubiquitin-proteasome pathway, thereby preventing their antiviral effects. The study of Vif and its interactions with host factors is essential for understanding HIV pathogenesis and the molecular mechanisms underlying viral evasion strategies. Research into Vif-recombinant proteins is pivotal for developing novel therapeutic strategies, including potential inhibitors that can restore the antiviral activity of APOBECs or otherwise impede HIV replication. Furthermore, Vif's unique structure and functional attributes make it an attractive target for vaccine design, as understanding its role could lead to innovations in immune responses against HIV. In this context, the recombinant production of Vif has become an important area of study, providing critical insights into its biochemical properties and facilitating the exploration of Vif-targeted interventions in HIV treatment.

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