Cat: IPD-X41378

Recombinant Human herpesvirus 6B U24 Protein ,His

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Analytical Data

  • Gene name

    U24

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    U24 protein

  • Species

    Human herpesvirus 6B

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9QJ42

  • Expression Region

    1-88aa

  • Molecular Weight

    16.2 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

U24 protein, a crucial component in various biological processes, has garnered significant attention due to its potential applications in biotechnology and medicine. Research on U24 protein began as scientists sought to understand its role in cellular mechanisms, particularly in relation to stress responses and metabolic regulation. Its unique structural properties suggest that it could play a role in protein folding, stability, and interaction with other biomolecules. Moreover, the U24 protein has been implicated in various diseases, raising the need for a deeper understanding of its function and mechanism. Recent advancements in recombinant DNA technology have enabled the production of U24 proteins in host systems, allowing for detailed studies on its functionality and potential therapeutic uses. This research is particularly relevant in the context of developing protein-based therapies, such as vaccines and enzyme replacement therapies. Given the growing interest in protein engineering and functional characterization, the study of U24 protein not only aims to elucidate its biological significance but also seeks to harness its properties for innovative applications in health and disease management. Understanding the dynamics of U24 protein and its interactions with other cellular components could pave the way for novel approaches in treating various conditions, underscoring the importance of ongoing research in this field.

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