Cat: PA1000-1583

Recombinant Human IL-1 Protein,His

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Analytical Data

  • Gene name

    IL-1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    IL37;FIL1Z;IL1F7;IL1H4;Interleukin-37

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P01584

  • Expression Region

    117-269aa

  • AA Sequence

    APVRSLNCTL RDSQQKSLVM SGPYELKALH LQGQDMEQQV VFSMSFVQGE ESNDKIPVAL GLKEKNLYLS CVLKDDKPTL QLESVDPKNY PKKKMEKRFV FNKIEINNKL EFESAQFPNW YISTSQAENM PVFLGGTKGG QDITDFTMQF VSS

  • Molecular Weight

    17 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-1 (IL-1) is a key pro-inflammatory cytokine involved in various immune responses, playing a crucial role in the pathogenesis of numerous diseases, including autoimmune disorders, inflammatory diseases, and cancer. Research on recombinant IL-1 proteins has gained significant attention due to their potential therapeutic applications. IL-1 exists in two main forms, IL-1α and IL-1β, both of which are synthesized as inactive precursors and require proteolytic cleavage for their activity. Investigating recombinant IL-1 proteins enables scientists to explore their biological functions, mechanisms of action, and signaling pathways, thereby advancing our understanding of inflammation and immune regulation. Furthermore, recombinant IL-1 proteins are valuable tools for studying the effects of this cytokine in vitro and in vivo, allowing for the development of novel therapies aiming to modulate IL-1 activity. For instance, IL-1 antagonists, such as anakinra, have already shown promise in treating conditions like rheumatoid arthritis. The exploration of IL-1's role in various diseases has also led to the identification of IL-1 as a potential target for immunotherapy, highlighting its importance in the evolving landscape of disease treatment strategies. Overall, the study of recombinant IL-1 proteins holds significant potential for advancing both basic and clinical research, providing insights that may translate into innovative therapeutic approaches.

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