Analytical Data
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Gene name
IL17
- Application
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Alternative Names
IL17A;CTLA8;IL17;Interleukin-17A
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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
Q16552
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Expression Region
20-155aa
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AA Sequence
MIVKAGITIP RNPGCPNSED KNFPRTVMVN LNIHNRNTNT NPKRSSDYYN RSTSPWNLHR NEDPERYPSV IWEAKCRHLG CINADGNVDY HMNSVPIQQE ILVLRREPPH CPNSFRLEKI LVSVGCTCVT PIVHHVA
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Molecular Weight
17 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-17 (IL-17) is a pro-inflammatory cytokine that plays a crucial role in the immune response, particularly in the context of autoimmune diseases, chronic inflammation, and infections. It is primarily produced by Th17 cells, a subset of CD4+ T cells that contribute to host defense against pathogens but can also lead to tissue damage when dysregulated. Research into IL-17 has gained momentum due to its involvement in various inflammatory disorders, including rheumatoid arthritis, psoriasis, and multiple sclerosis. As a result, IL-17 and its signaling pathways have become attractive targets for therapeutic intervention. The development of recombinant IL-17 proteins has enabled researchers to study the cytokine's structure and function in greater detail. These recombinant proteins can be used in vitro to investigate their effects on immune cells and to elucidate the mechanisms underlying IL-17-mediated inflammation. Furthermore, recombinant IL-17 is also instrumental in preclinical and clinical studies aimed at developing IL-17 inhibitors, which have shown promise in treating several inflammatory diseases. Understanding the biological role of IL-17, along with the development of targeted therapies, holds significant potential for improving outcomes for patients suffering from IL-17-associated conditions. Thus, research on IL-17 recombinant proteins is vital for advancing therapeutic strategies and enhancing our understanding of immune regulation and inflammatory diseases.
