Analytical Data
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Gene name
IL1R2
- Application
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Alternative Names
IL1R2;IL1RB;Interleukin-1 receptor type 2
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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
P27930
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Expression Region
14-343aa
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AA Sequence
FTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPYWLWASVSP RINLTWHKND SARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTR NASYCDKMSIELRVFENTDAFL PFISYPQILTLSTSGVLVCPDLSEFT RDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLL VHDVALEDAGYYRC VLTFAHEGQQYNITRSIELRIKKKKEETIPVIISPLKTISASLGSR LT IPCKVFLGTGTPLTTMLWWTANDTHIESAYPGGRVTEGPRQEYSENNENY IEVPLIFD PVTREDLHMDFKCVVHNTLSFQTLRTTVKE
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Molecular Weight
39 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-1 receptor type 2 (IL1R2) is a critical member of the interleukin-1 receptor family, primarily known for its role as a decoy receptor that binds interleukin-1 (IL-1) cytokines, thereby modulating inflammatory responses. It can inhibit IL-1 signaling by preventing IL-1 from interacting with its primary signaling receptor, IL1R1. Research into IL1R2 has gained momentum due to its potential therapeutic applications in various inflammatory diseases, autoimmune disorders, and cancer. Recombinant IL1R2 protein has been developed to explore its mechanisms of action and therapeutic potential. Studies have indicated that by saturating the pro-inflammatory environment with IL1R2, it may be possible to reduce tissue damage and limit chronic inflammation. Additionally, understanding the structure-function relationship of IL1R2 can aid in the design of new therapeutic agents aimed at enhancing its inhibitory effects on IL-1 signaling. Given the pivotal role of IL-1 in numerous pathological conditions, recombinant IL1R2 presents a promising area of research, potentially leading to novel anti-inflammatory therapies and improved management of diseases characterized by excessive IL-1 activity.











