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Recombinant Human IL-1 RII Fc Chimera Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 663-2R

R&D Systems, part of Bio-Techne
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663-2R-050

Key Product Details

Source

CHO

Accession #

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human IL-1 RII protein
Human IL-1 RII
(His21 - Glu343)
Accession # P27930
IEGRMD Human IgG1
(Pro100 - Lys330)
N-terminus C-terminus

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.01 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

His21

Predicted Molecular Mass

63.7 kDa (monomer)

SDS-PAGE

80-95 kDa, reducing conditions

Activity

Measured by its ability to inhibit IL-1 beta-dependent proliferation in D10.G4.1 mouse helper T cells. Symons, J.A. et al. (1987) in Lymphokines and Interferons, a Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 272.

Approximately 0.3-1.8 μg/mL of Recombinant Human (rh) IL‑1 RII Fc Chimera will inhibit 50% of the biological response due to 50 pg/mL of rhIL-1 beta.

Formulation, Preparation and Storage

663-2R
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 100 μg/mL in PBS.

Reconstitution Buffer Available:
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Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: IL-1 RII

IL-1 Receptor II (also IL‑1 R2) is a 60 ‑ 70 kDa member of the interleukin‑1 receptor family of proteins (1 ‑ 4). It serves as a non‑signaling ligand‑binding decoy receptor for IL‑1 beta and IL‑1 alpha (4). IL‑1 binds to a cell surface complex composed of IL‑1 RI and IL‑1 RAcP. Upon activation, this complex recruits MyD88 for downstream signaling (4, 5). The proinflammatory action of IL-1 is antagonized by IL‑1ra which binds to IL‑1 RI but does not initiate signaling. A second natural antagonist is IL‑1 RII, a cell surface receptor that binds both IL‑1 alpha and beta, but not IL‑1ra. IL‑1 RII is found on astrocytes, neutrophils, anterior pituitary acidophils that secrete GH, corneal epithelium, testicular Leydig and Sertoli cells, B cells and monocytes/macrophages (6 ‑ 12). Mature human IL‑1 RII is a 385 amino acid (aa) type I transmembrane glycoprotein that contains a 330 aa extracellular region with three Ig‑like domains (aa 14 ‑ 343), a 26 aa transmembrane segment, and a 29 aa cytoplasmic domain with no signaling motifs (13). There is one soluble 55 ‑ 60 kDa alternative splice form that shows a premature truncation after Gln296 (14). ARTS‑1 mediated cleavage of IL-1 RII generates a 47 kDa isoform, while alpha‑secretase cleavage after Arg338 creates a 50 ‑ 55 kDa isoform that undergoes further processing back to Pro314 (15, 16). Human IL‑1 RII shares 59% aa identity with mouse IL‑1 RII in the extracellular region. Different forms of human IL‑1 RII demonstrate differing binding affinities for IL‑1. IL‑1 RII has a preference for IL‑1 beta over IL‑1 alpha, and binding requires the presence of IL‑1 RAcP. This interaction prevents the association of IL‑1 with IL‑1 RI and also restricts IL‑1 R to a non‑signaling receptor complex (11, 17 ‑ 19). The membrane IL‑1 RII:IL‑1 RAcP complex does not form a functional bond with IL‑1ra, and cannot bind pro‑IL‑1 beta (11, 13, 19, 20). Soluble IL‑1 RII, by contrast, demonstrates a different binding profile. Notably, it will bind pro‑IL‑1 beta rendering it unavailable for activation by extracellular proteases (19, 20). Although it will sequester both IL‑1 beta and IL‑1 alpha, its interaction with soluble IL‑1 RAcP creates a circulating high affinity complex for both IL‑1 beta and IL‑1 alpha, thus potentiating its anti‑inflammatory activity.

References

  1. Dinarello, C.A. (2011) Blood 117:3720.
  2. Boraschi, D. and A. Tagliabue (2006) Vitam. Horm. 74:229.
  3. Dunne, A. and L.A.J. O’Neill (2003) Sci STKE. Feb 25;2003(171):re3.
  4. Dinarello, C.A. (2009) Annu. Rev. Immunol. 27:519.
  5. O’Neill, L.A.J. (2008) Immunol. Rev. 226:10.
  6. Pousset, F. et al. (2001) J. Neurochem. 79:726.
  7. Bourke, E. et al. (2003) J. Immunol. 170:5999.
  8. French, R.A. et al. (1996) Endocrinology 137:4027.
  9. Cubitt, C.L. et al. (2001) Invest. Ophthalmol. Vis. Sci. 42:701.
  10. Gomez, E. et al. (1997) Biol. Reprod. 56:1513.
  11. Lang, D. et al. (1998) J. Immunol. 161:6871.
  12. Mantovani, A. et al. (2001) Trends Immunol. 22:328.
  13. McMahan, C.J. et al. (1991) EMBO J. 10:2821.
  14. Liu, C. et al. (1996) J. Biol. Chem. 271:20965.
  15. Cui, X. et al. (2003) J. Immunol. 171:6814.
  16. Kuhn, P-H. et al. (2007) J. Biol. Chem. 282:11982.
  17. Smith, D.E. et al. (2003) Immunity 18:87.
  18. Makinowsky, D. et al. (1998) FEBS Lett. 429:299.
  19. Neumann, D. et al. (2000) J. Immunol. 165:3350.
  20. Symons, J. A. et al. (1995) Proc. Natl. Acad. Sci. USA 92:1714.
  21. Wang, D. et al. (2010) Nat. Immunol. 11:905.

Long Name

Interleukin 1 Receptor II

Alternate Names

CD121b, IL-1 R beta, IL-1RII, IL1R2, IL1RII

Entrez Gene IDs

7850 (Human); 16178 (Mouse)

Gene Symbol

IL1R2

UniProt

Additional IL-1 RII Products

Product Documents for Recombinant Human IL-1 RII Fc Chimera Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human IL-1 RII Fc Chimera Protein, CF

For research use only

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