Analytical Data
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Gene name
IL23
- Application
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Alternative Names
IL23；Interleukin-23 receptor
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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
Q9NPF7
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Expression Region
23-328aa
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AA Sequence
IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCSGSTS GSGKPGSGEG STKGRAVPGG SSPAWTQCQQ LSQKLCTLAW SAHPLVGHMD LREEGDEETT NDVPHIQCGD GCDPQGLRDN SQFCLQRIHQ GLIFYEKLLG SDIFTGEPSL LPDSPVGQLH ASLLGLSQLL QPEGHHWETQ QIPSLSPSQP WQRLLLRFKI LRSLQAFVAV AARVFAHGAA TLSP
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Molecular Weight
70 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-23 (IL-23) is a pro-inflammatory cytokine that plays a critical role in the immune response and the pathogenesis of various autoimmune diseases. It is primarily produced by activated dendritic cells and macrophages and is essential for the maintenance of T helper 17 (Th17) cell populations, which are implicated in conditions such as psoriasis, inflammatory bowel disease, and multiple sclerosis. The interest in IL-23 has surged due to its role in driving chronic inflammation and tissue damage, prompting extensive research into its potential as a therapeutic target. Recombinant IL-23 proteins have been developed to explore their biological functions and therapeutic applications. Understanding the structure, function, and signaling pathways of IL-23 is crucial for the design of new biologic therapies aimed at modulating the immune response. Studies involving IL-23 recombinant proteins help elucidate the complex interplay between cytokines and immune cells, providing insights that can lead to innovative treatments for autoimmune and inflammatory disorders. Moreover, the development of IL-23 inhibitors, such as monoclonal antibodies, has shown promise in clinical settings, demonstrating the importance of IL-23 in both basic research and clinical applications. Overall, ongoing investigations into IL-23 and its recombinant forms continue to advance our knowledge of immune regulation and offer potential pathways for novel therapeutic interventions.
