Cat: IPD-X41032

Recombinant Human herpesvirus 6A U27 Protein (Yeast),His

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Analytical Data

  • Gene name

    U27

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Phosphoprotein P41 ;PP41;Polymerase accessory protein ;PAP

  • Species

    Human herpesvirus 6A

  • Source

    Yeast

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P52439

  • Expression Region

    1-393aa

  • Molecular Weight

    46.8 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

U27 recombinant protein research is situated within the broader context of understanding viral oncogenesis and the immune evasion mechanisms of certain pathogens. The U27 gene, derived from the Epstein-Barr virus (EBV), encodes a protein that has been implicated in the regulation of host cell growth and apoptosis, making it a critical player in the virus's ability to promote tumorigenesis. EBV is associated with various malignancies, including Hodgkin's lymphoma and nasopharyngeal carcinoma, thus underscoring the need for in-depth studies on its genetic components. The recombinant expression of U27 protein facilitates the investigation of its functional roles in cellular pathways, immune response modulation, and its potential interactions with host proteins. By elucidating the mechanisms by which U27 influences host cell behavior, researchers aim to find novel therapeutic targets and enhance our understanding of viral contributions to cancer biology. This research is not only important for the development of antiviral strategies but also for the design of vaccines and other immunotherapies that could mitigate the impact of EBV-driven diseases. Overall, U27 recombinant protein studies highlight the interplay between viral proteins and host cellular machinery, offering insights that are crucial for advancing cancer research and improving patient outcomes.

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