Cat: IPD-X10944

Recombinant Horse IL-11 Protein , Two N- s, His- & SUMO-

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Analytical Data

  • Gene name

    IL-11

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    AGIF; Adipogenesis Inhibitory Factor; Oprelvekin

  • Species

    Horse

  • Source

    E. coli

  • Tag

    Two N- s, His- & SUMO-

  • Purity

    > 80% as determined by SDS-PAGE.

  • Uniprot

    XM_005596548.2

  • Expression Region

    Ala58~Leu199

  • Molecular Weight

    34kDa

  • 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 11 (IL-11) is a member of the interleukin-6 (IL-6) family of cytokines and plays a crucial role in various physiological and pathological processes, including inflammation, tissue repair, and fibrosis. Initially identified for its role in promoting megakaryocyte development and platelet production, IL-11 has gained attention in recent years due to its involvement in pathological conditions such as chronic inflammatory diseases, cancer, and fibrotic disorders. The study of recombinant IL-11 proteins has become significant in understanding its biological functions and therapeutic potential. Research has shown that IL-11 can modulate immune responses, influencing T cell differentiation and activation. Moreover, its profibrotic properties make it a candidate for studying the mechanisms underlying organ fibrosis and developing targeted therapies. Recombinant IL-11 proteins are being investigated for their use in clinical settings, particularly for their potential to mitigate inflammation or promote tissue healing. The development of IL-11 as a therapeutic agent highlights the need for advanced recombinant protein production technologies to ensure safety, efficacy, and bioactivity. Overall, the research surrounding IL-11 recombinant proteins is essential for unraveling their complex roles in health and disease, paving the way for innovative treatment strategies that harness the unique properties of this cytokine.

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