Cat: IPD-X39577

Recombinant Human RNASE9 Protein,His

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Analytical Data

  • Gene name

    RNASE9

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Inactive ribonuclease-like protein 9

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P60153

  • Expression Region

    Leu28~Pro210

  • Molecular Weight

    25kDa

  • 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

RNASE9, a member of the ribonuclease A superfamily, has garnered attention in recent years due to its unique structural features and potential biological functions. It is particularly notable for its ability to degrade RNA, which places it in a crucial role in various cellular processes such as RNA turnover, gene regulation, and antiviral defense mechanisms. Understanding the properties of RNASE9 and its functional implications could provide valuable insights into its role in human diseases, particularly in conditions associated with dysregulated RNA metabolism. Moreover, the recombinant expression of RNASE9 allows for the production of substantial quantities of the protein for in-depth biochemical studies and therapeutic applications. Given the increasing interest in RNA-based therapies and the potential for targeting RNA-utilizing pathways in disease, RNASE9 is positioned as a promising candidate for further exploration. Its evolutionary adaptations and specific activity against various RNA substrates suggest diverse functional roles, making it a fascinating subject for research aimed at delineating its physiological significance and exploiting its capabilities in biotechnological applications. As researchers continue to investigate the molecular mechanisms underlying RNASE9's activity, the prospects for harnessing this protein for novel therapeutic strategies become increasingly viable.

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