Cat: IPD-X32405

Recombinant Human DHX9 Protein (HEK293),Flag & Myc

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Analytical Data

  • Gene name

    DHX9

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    DEAH box protein 9Leukophysin ;LKPNuclear DNA helicase II ;NDH II

  • Species

    Human

  • Source

    HEK293

  • Tag

    C- Flag-Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q08211

  • Expression Region

    325-840aa

  • Molecular Weight

    61.6 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

DHX9, a member of the DExH-box family of RNA helicases, plays a crucial role in various cellular processes including transcription, RNA processing, and regulation of gene expression. Its involvement in the unwinding of RNA structures makes it essential in modulating the function of diverse RNA molecules. Recent studies have indicated that DHX9 is linked to several diseases, including cancer and viral infections, highlighting its potential as a therapeutic target. The production of recombinant DHX9 protein has emerged as an important strategy to study its biochemical properties and interactions. By utilizing advanced techniques such as recombinant DNA technology, researchers can produce large quantities of DHX9 in host cells, facilitating detailed investigations into its enzymatic activity and structural characteristics. Understanding the dynamics of DHX9 at a molecular level could provide insights into its role in pathophysiology and uncover novel avenues for drug development, particularly in targeting RNA-based diseases. Furthermore, the exploration of DHX9’s interaction with other proteins and RNA elements can elucidate its multifaceted functions in cellular regulation and stress responses. Overall, the research on recombinant DHX9 protein is critical for advancing our knowledge of RNA biology and its implications for health and disease.

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