IL-1R2 Protein, Human (HEK293, His)

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, His) is a recombinant human IL-1R2 protein with a His tag at the C-terminus and is expressed in HEK293 cells. It consists of 330 amino acids (F14-E343).

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].

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].

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].

Human

HEK293

C-His

P27930/NP_004624.1 (F14-E343)

7850  [NCBI]

Extracellular Domain

FTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPYWLWASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFLPFISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRIKKKKEETIPVIISPLKTISASLGSRLTIPCKVFLGTGTPLTTMLWWTANDTHIESAYPGGRVTEGPRQEYSENNENYIEVPLIFDPVTREDLHMDFKCVVHNTLSFQTLRTTVKE

Approximately 50 kDa

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.

• [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]