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, Mouse (HEK293, His) is a recombinant mouse IL-1R2 protein with a His tag at the C-terminus and is expressed in HEK293 cells. It consists of 342 amino acids (F14-E355).

IL-1R2 is the non-signaling type 2 interleukin-1 receptor and is expressed in DC, CD4+ T cells, T regulatory cells, monocytes, neutrophils and different macrophagic cells in mouse. The mouse IL-1R2 can be cleaved into two forms: membrane form (14-410 a.a) and soluble form (14-? a.a).
The sequence of amino acids in IL-1R2 from mouse shows low similarity (about 60%) with human IL-1R2, but has been only slightly altered with rat IL-1R2 (90 % similarity).
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.

IL-1R2 (24 h) specifically inhibits IL-1β-induced urokinase-type plasminogen activator responses in HUVECs.

IL-1R2 knockout mice exacerbates cardiac damage in myocardial ischemia reperfusion (I/R) injury and knockout of IL-1R2 induces cytokines expression in the heart after I/R injury.
AAV9-IL-1R2 (40 µL; myocardial injection, once) protects heart against IL-17A-induced cardiomyocytes apoptosis through suppressing IL-17RA expression in mice.

Mouse

HEK293

C-6*His

P27931 (F14-E355)

16178  [NCBI]

FTTPTVVHTGKVSESPITSEKPTVHGDNCQFRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSFLTWSKLDSSQLIPRDEPRMWVKGNILWILPAVQQDSGTYICTFRNASHCEQMSVELKVFKNTEASLPHVSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQEYNITRNIELRVKGTTTEPIPVIISPLETIPASLGSRLIVPCKVFLGTGTSSNTIVWWLANSTFISAAYPRGRVTEGLHHQYSENDENYVEVSLIFDPVTREDLHTDFKCVASNPRSSQSLHTTVKE

45-60 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 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. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer. It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

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  [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]. Simeoni E, et al. Gene transfer of a soluble IL-1 type 2 receptor-Ig fusion protein improves cardiac allograft survival in rats. Eur J Cardiothorac Surg. 2007 Feb;31(2):222-8.  [Content Brief]