Cat: IPD-X10548

Recombinant Human IL-30 Protein , N-His

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Analytical Data

  • Gene name

    IL-30

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    p28; IL30; Interleukin 30; Interleukin-27 subunit alpha; IL-27 subunit alpha; IL27-A

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    > 95% as determined by SDS-PAGE.

  • Uniprot

    Q8NEV9

  • Expression Region

    Met1~Glu173

  • Molecular Weight

    36kDa

  • 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

Interleukin-30 (IL-30), a recently identified member of the interleukin-6 cytokine family, plays a critical role in the immune response and has gained attention for its potential therapeutic applications. Research indicates that IL-30 is predominantly expressed in activated T cells and has been implicated in various inflammatory and autoimmune diseases. Its unique ability to regulate the activity of immune cells and modulate inflammatory responses makes it a candidate for further exploration in disease contexts, particularly those characterized by excessive inflammation or dysregulated immune function. Additionally, recombinant IL-30 protein has been produced to facilitate detailed studies regarding its biological functions and signaling pathways. Understanding the mechanisms of IL-30's action could provide insights into novel treatment strategies for conditions such as rheumatoid arthritis, multiple sclerosis, and other immune-mediated disorders. Furthermore, the development of IL-30-based therapies may enhance the efficacy of existing treatments and improve patient outcomes in chronic inflammatory diseases. As research progresses, characterization of IL-30’s interactions with other cytokines and its role in immune cell differentiation remains a focal point, offering avenues for targeted interventions and biomarker discovery. Overall, the investigation of IL-30 and its recombinant form holds promise in the realm of immunotherapy and precision medicine, underscoring the importance of cytokine biology in managing complex diseases.

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