IL-1R2 Protein, Human (HEK293)
Based on 1 Customer Validation
IL-1R2 is a competitive endogenous inhibitor of IL-1 signaling. IL-1R2 serves as a decoy receptor and competes with IL-1R1 for IL-1, it can also form a complex with IL-1RAP once it binds IL-1. IL-1R2 is implicated in various IL-1-mediated inflammatory diseases. IL-1R2 Protein, Human (HEK293) is a recombinant human IL-1R2 protein and is expressed in HEK293 cells. It consists of 343 amino acids (M1-E343).
- Species: Human
- Source: HEK293
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Biological Activity
Description
IL-1R2 is a competitive endogenous inhibitor of IL-1 signaling. IL-1R2 serves as a decoy receptor and competes with IL-1R1 for IL-1, it can also form a complex with IL-1RAP once it binds IL-1. IL-1R2 is implicated in various IL-1-mediated inflammatory diseases[1]. IL-1R2 Protein, Human (HEK293) is a recombinant human IL-1R2 protein and is expressed in HEK293 cells. It consists of 343 amino acids (M1-E343).
Background
IL-1R2 is the non-signaling type 2 interleukin-1 receptor and is natively found on neutrophils, B-cells, monocytes and macrophages. IL-1R2 is also expressed in breast and colon cancer cells. IL-1R2 is rapidly upregulated in human regulatory T cells (Tregs). The human IL-1R2 can be cleaved into two forms: membrane form (14-398 a.a) and soluble form (14-? a.a).
The sequence of amino acids in IL-1R2 from human shows low similarity (about 60%) with both mouse and rat IL-1R2.
IL-1R2 contains truncated cytoplasmic domain and lacks Toll-IL-1 receptor (TIR) region, making it incapable of transmembrane signaling. IL-1R2 serves as an endogenous inhibitor of IL-1 signaling. Functional IL-1 signaling requires IL-1R1 and IL-1-dependent recruitment of IL-1RAP. IL-1R2 serves as a decoy receptor and can compete with IL-1R1 for IL-1. IL-1R2 can also form a complex with IL-1RAP once it binds IL-1, preventing IL-1RAP from heterodimerizing with IL-1R1. Through these 2 ways, IL-1R2 blocks IL-1 signaling. Additionally, soluble IL-1R2 recruits soluble IL-1RAP with high affinity without impacting affinity for IL-1RA.
IL-1R2 inhibits IL-1 signaling and has been implicated in various IL-1-mediated inflammatory diseases like arthritis, diabetes, gout and so on[1][2][3].
In Vitro
IL-1R2 but not IL-1R1 or IL-1RAcP is sensitive to PMA-induced proteolytic activity and ectodomain shedding of IL-1R2 is dependent on ADAM17[5].
In Vivo
Human sIL-1R2 (5 or 25 μg/kg; i.p.; daily for 24 days) decreases the development of endometrial implants and inflammation in mice[4].
Verified Bioactivity
Immobilized Human IL-1R2, No Tag at 2 μg/mL (100 μl/well) on the plate. Dose response curve for Biotinylated Human IL-1 Beta, His Tag with the EC50 of 0.21 μg/mL determined by ELISA.
Technical Parameters
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Species Human
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Source HEK293
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Tag Tag Free
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Accession
P27930 (F14-E343)
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Molecular Construction
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N-term
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IL-1R2 (F14-E343)
Accession # P27930 -
C-term
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Protein Length
Extracellular Domain
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Synonyms
IL1R2; IL-1RT-2; Prev. IL1RB; IL-1R-2; CD121b; IL-1RT2; CD121 Antigen-Like Family Member B; Type II Interleukin-1 Receptor, Beta; Interleukin-1 Receptor Type II; Interleukin 1 Receptor, Type II; Interleukin-1 Receptor Type 2; Antigen CDw121b; Interleukin-
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AA Sequence
FTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPYWLWASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFLPFISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRIKKKKEETIPVIISPLKTISASLGSRLTIPCKVFLGTGTPLTTMLWWTANDTHIESAYPGGRVTEGPRQEYSENNENYIEVPLIFDPVTREDLHMDFKCVVHNTLSFQTLRTTVKE
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Predicted Molecular Mass
37.8 kDa
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Molecular Weight
Approximately 49-70 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.
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Glycosylation
Yes
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Purity
≥ 95%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (265 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
References
[1]. PetersVA,etal.IL-1receptor2(IL-1R2)anditsroleinimmuneregulation.BrainBehavImmun.2013Aug;32:1-8. [Content Brief]
[2]. Molgora M, et al. Tuning inflammation and immunity by the negative regulators IL-1R2 and IL-1R8. Immunol Rev. 2018 Jan;281(1):233-247. [Content Brief]
[3]. Lin J, et al. Cardiomyocyte IL-1R2 protects heart from ischemia/reperfusion injury by attenuating IL-17RA-mediated cardiomyocyte apoptosis. Cell Death Dis. 2022 Jan 27;13(1):90. [Content Brief]
[4]. Khoufache K, et al. Soluble human IL-1 receptor type 2 inhibits ectopic endometrial tissue implantation and growth: identification of a novel potential target for endometriosis treatment. Am J Pathol. 2012 Oct;181(4):1197-205. [Content Brief]
[5]. Uchikawa S, et al. ADAM17 regulates IL-1 signaling by selectively releasing IL-1 receptor type 2 from the cell surface. Cytokine. 2015 Feb;71(2):238-45. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)