Cat: PA1000-1591

Recombinant Human IL-2 Protein,His

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Analytical Data

  • Gene name

    IL-2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    IL2RA;Interleukin-2 receptor subunit alpha

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P60568

  • Expression Region

    21-153aa

  • AA Sequence

    APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT

  • Molecular Weight

    41.5 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.

Quality inspection process

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Protein Description

Interleukin-2 (IL-2) is a key cytokine that plays a crucial role in the immune response, particularly in the proliferation and activation of T cells. It was first discovered in the late 1970s and has since been recognized for its therapeutic potential in various diseases, including cancer and autoimmune disorders. Due to its significant role in immune regulation, research on recombinant IL-2 has gained momentum, especially in the context of immunotherapy. Recombinant DNA technology has enabled the production of high-purity IL-2 for both research and clinical applications. This has opened avenues for investigating its use as an adjuvant in cancer vaccination, enhancing the efficacy of anti-tumor responses by promoting T cell expansion and activity. Moreover, IL-2 has been utilized in combination therapies to synergize with other immune-modulating agents. However, its clinical use is limited by adverse effects such as vascular leak syndrome and dose-dependent toxicity. As a result, ongoing research aims to develop safer IL-2 variants, optimize dosing regimens, and explore novel delivery methods to maximize its therapeutic benefits while minimizing side effects. Investigations into the mechanisms of action of IL-2 at the cellular and molecular levels are also being conducted to better understand its role in immune responses. Overall, the study of recombinant IL-2 continues to be a significant area of interest, contributing to advancements in immunotherapy and the development of novel treatment strategies for cancer and other immune-related conditions.

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