Analytical Data
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Gene name
IL18
- Application
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Alternative Names
IL18;IGIF;IL1F4;Interleukin-18
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14116
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Expression Region
37-193aa
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AA Sequence
MYFGKLESKLSVIRNLNDQVLFIDQGNRPLFEDMTDSDCRDNAPRTIFII SMYKDSQPRGMAVTISVKCEKISTLSCENKIISFKEMNPPDNIKDTKSDI IFFQRSVPGHDNKMQFESSSYEGYFLACEKERDLFKLILKKEDELGDRSI MFTVQNED
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Molecular Weight
19 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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-18 (IL-18) is a pro-inflammatory cytokine that plays a crucial role in the immune response, particularly in promoting the production of interferon-gamma (IFN-γ) from T and natural killer (NK) cells. Initially discovered for its ability to induce IFN-γ production, IL-18 is produced as a precursor and requires cleavage by caspase-1 for its activation. The cytokine is involved in various physiological processes, including the regulation of Th1 responses, enhancement of innate immunity, and modulation of inflammatory diseases. Due to its significant role in immune regulation, IL-18 has been studied in the context of several conditions, including infectious diseases, autoimmune disorders, and cancer. The research on recombinant IL-18 protein has gained traction as scientists seek to examine its therapeutic potential and underlying mechanisms of action. Recombinant forms of IL-18 are essential for in vitro studies, allowing researchers to explore its effects on immune cell behavior, cytokine production, and potential synergies with other immunotherapeutics. Furthermore, the development of IL-18 as a candidate for cancer immunotherapy is particularly promising, given its ability to enhance anti-tumor immune responses. However, the dual role of IL-18 in promoting both protective and pathological immune responses underscores the complexity of its application in clinical settings. Ongoing studies aim to elucidate the precise mechanisms by which IL-18 influences various immune pathways, as well as optimizing its therapeutic applications while minimizing potential adverse effects. Overall, the continued exploration of recombinant IL-18 protein is vital for advancing our understanding of immune regulation and developing novel therapeutic strategies for immune-related diseases.
