Cat: IPD-X41485

Recombinant African swine fever virus Ba71V-126 Protein ,His

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Analytical Data

  • Gene name

    Ba71V-126

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (pE183L)

  • Species

    African swine fever virus

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q65194

  • Expression Region

    54-183aa

  • Molecular Weight

    17.8 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

The Ba71V-126 recombinant protein is a significant focus of research due to its potential implications in virology and immunology. Derived from the Ba71V strain of virulent vesicular stomatitis virus (VSV), this protein has garnered attention for its ability to evoke immune responses that could be harnessed for therapeutic applications. The study of Ba71V-126 is particularly pertinent in the context of vaccine development, as it may serve as a promising candidate for enhancing immunity against various viral infections. Researchers are investigating its structure-function relationships, the mechanisms by which it stimulates immune responses, and its efficacy in preclinical models. Moreover, the recombinant expression of Ba71V-126 allows for the exploration of potential adjuvants and delivery systems that could optimize its immunogenic properties. As such, research on this recombinant protein not only contributes to a deeper understanding of VSV biology but also paves the way for innovative approaches to vaccine design and the development of therapeutic strategies against viral diseases. The ongoing studies aim to elucidate the precise role of Ba71V-126 in eliciting protective immune responses, ultimately targeting its application in human health and disease prevention. The findings could have far-reaching consequences for vaccine technologies and the broader field of infectious disease research.

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