Cat: IPD-X39623

Recombinant Human RNASE11 Protein,His

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Analytical Data

  • Gene name

    RNASE11

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    C14orf6

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8TAA1

  • Expression Region

    Ala18~Leu199

  • Molecular Weight

    24kDa

  • 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

RNase A family members, including RNASE11, have garnered significant attention due to their roles in various biological processes and potential therapeutic applications. RNASE11, a ribonuclease enzyme, is part of the larger RNase A superfamily, which is known for its ability to degrade RNA and play roles in antimicrobial activity, cell signaling, and immune response. Recent studies suggest that RNASE11 may also be involved in the regulation of apoptosis and the potential modulation of inflammatory responses. Despite its intriguing biological functions, the precise biochemical properties and mechanisms of action of RNASE11 remain under-explored. The recombinant expression of RNASE11 in various systems offers a pathway to investigate its structure-function relationship, substrate specificity, and interactions with other biomolecules. Such studies aim to elucidate the potential of RNASE11 in molecular biology and medicine, including its role in cancer biology and its application in therapeutic enzyme development. Understanding the functional aspects of RNASE11 can provide insights into its utility as a diagnostic or therapeutic agent, making it a subject of increasing interest in biomedical research. Moreover, elucidating the biochemical pathways involving RNASE11 can contribute to a broader understanding of RNA metabolism and its impact on cellular homeostasis. Given the expanding significance of ribonucleases in therapeutic contexts, RNASE11 representation as a recombinantly produced protein is a promising avenue for exploration within modern molecular biology and biochemistry.

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