Recombinant Human IL-36Ra/IL-1F5 Protein

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Recombinant HumanIL-36Ra/IL-1F5(Catalog # 1275-IL) inhibits Recombinant Human IL-36 beta/IL-1F8 (Catalog # 6834-ILB) induced IL-8 secretionby A431 human epithelial carcinoma cells. The ED50 for this effect is0.2-1 ...read more

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Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human IL-36Ra/IL-1F5 Protein Summary

Details of Functionality
Measured by its ability to inhibit IL-36 alpha, IL-36 beta or IL-36 gamma -induced IL-8 secretion in A431 human epithelial carcinoma cells. The ED50 for this effect is 0.2-1 μg/mL in the presence of 10 ng/mL of recombinant human IL-36 beta.
Source
E. coli-derived human IL-36Ra/IL-1F5 protein
Val2-Asp155
Accession #
N-terminal Sequence
Val2
Protein/Peptide Type
Recombinant Proteins
Gene
IL36RN
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
17 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using
1275-IL in the following applications:

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-36Ra/IL-1F5 Protein

  • FIL1 delta
  • FIL1
  • FIL1-delta, IL-1RP3, IL-1L1, IL-1-delta)
  • FIL1DIL-1 delta
  • IL1F5 (Canonical product IL-1F5a)
  • IL1F5
  • IL-1HY1
  • IL-1L1
  • IL-1RP3
  • IL36Ra
  • IL-36Ra
  • IL36RN
  • interleukin 1 family, member 5 (delta)
  • interleukin 1, delta
  • Interleukin 36 Receptor Antagonist
  • interleukin-1 family member 5
  • Interleukin-1 HY1
  • Interleukin-1 receptor antagonist homolog 1
  • Interleukin-1-like protein 1
  • Interleukin-36 Receptor Antagonist

Background

Human interleukin-36 receptor antagonist [IL-36Ra; previously IL-1F5 and also named FIL-1δ (delta), IL‑1HY1, IL‑1H3, and IL-1L1] is a member of the IL‑1 family of proteins (1 ‑ 6). IL‑1 family members include IL-1 beta, IL-1 alpha, IL-1ra, IL‑18 and IL-1F5-F10 (7). All family members show a 12 beta -strand, beta -trefoil configuration, and all family members are believed to have arisen from a common ancestral gene that underwent multiple duplications (7). The human IL‑36Ra/IL‑1F5 gene is in closest proximity to the gene for IL-1ra and is likely a relatively recent duplication of the IL-1ra gene (2, 3). IL-36Ra/IL-1F5 is synthesized as a 155 amino acid (aa) protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation site(s) (2 - 5). Nevertheless, it appears to be secreted as a 17 kDa monomer (5). There is an alternate start site that potentially gives rise to an alternate splice form (5). The translated product, however, has a premature stop codon, resulting in a truncated 16 aa peptide. Human to mouse, full length IL-1F5 has 90% aa identity. Within the family, IL-36Ra/IL-1F5 is 50% aa identical to IL-1ra, and 32%, 31%, 35%, 37%, 32% and 42% aa identical to IL-1 beta, IL-36 alpha /IL‑1F6, IL‑37/IL‑1F7, IL‑36 beta /IL‑1F8, IL‑36 gamma /IL‑1F9 and IL‑1F10, respectively. Cells reported to express
IL‑36Ra/IL‑1F5 include monocytes, B cells, dendritic cells/Langerhans cells, keratinocytes, and gastric fundus Parietal and Chief cells (1, 8). The receptor for
IL-36Ra/IL-1F5 has not been positively identified. Indirect evidence suggests it is IL-1 Rrp2 and/or IL-1 RAcP (9). In either case, activity association with receptor binding is also unclear. It was initially reported to be an antagonist of IL‑36 gamma /IL‑1F9 activity (4, 6). This would be consistent with its hypothesized relationship to
IL‑1ra. Studies, however, find IL-36Ra/IL-1F5 antagonist activity difficult to demonstrate (9).

  1. Smith, D. E. et al. (2000) J. Biol. Chem. 275:1169.
  2. Kumar, S. et al. (2000) J. Biol. Chem. 275:10308.
  3. Mulero, J.J. et al. (1999) Biochem. Biophys. Res. Commun. 263:702.
  4. Nicklin, M.J.H. et al. (2002) Genomics. 79:718.
  5. Barton, J.L. et al. (2000) Eur. J. Immunol. 30:3299.
  6. Dinarello, C. et al. (2010) Nat. Immunol. 11:973.
  7. Dunn, E. et al. (2001) Trends Immunol. 22:533.
  8. Debets, R. et al. (2001) J. Immunol. 167:1440.
  9. Towne, J.E. et al. (2004) J. Biol. Chem. 279:13677.

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1275-IL
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Applications: Bioactivity

Publications for IL-36Ra/IL-1F5 (1275-IL)(7)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 2 applications: Binding Assay, Bioassay.


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Binding Assay
(1)
Bioassay
(6)
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Human
(7)
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Showing Publications 1 - 7 of 7.
Publications using 1275-IL Applications Species
L Mercurio, CM Failla, L Capriotti, C Scarponi, F Facchiano, M Morelli, S Rossi, G Pagnanelli, C Albanesi, A Cavani, S Madonna Interleukin (IL)-17/IL-36 axis participates to the crosstalk between endothelial cells and keratinocytes during inflammatory skin responses PLoS ONE, 2020;15(4):e0222969. 2020 [PMID: 32352958] (Bioassay, Human) Bioassay Human
L Mercurio, M Morelli, C Scarponi, EZ Eisenmesse, N Doti, G Pagnanelli, E Gubinelli, C Mazzanti, A Cavani, M Ruvo, CA Dinarello, C Albanesi, S Madonna IL-38 has an anti-inflammatory action in psoriasis and its expression correlates with disease severity and therapeutic response to anti-IL-17A treatment Cell Death Dis, 2018;9(11):1104. 2018 [PMID: 30377293] (Bioassay, Human) Bioassay Human
J Zhang, Y Yin, X Lin, X Yan, Y Xia, L Zhang, J Cao IL-36 induces cytokine IL-6 and chemokine CXCL8 expression in human lung tissue cells: Implications for pulmonary inflammatory responses Cytokine, 2017;99(0):114-123. 2017 [PMID: 28869889] (Bioassay, Human) Bioassay Human
V Schmitt, M Hahn, V Kästele, O Wagner, M Wiendl, A Derer, A Taddeo, S Hahne, A Radbruch, HM Jäck, W Schuh, D Mielenz, S Gay, G Schett, AJ Hueber, S Frey Interleukin-36 receptor mediates the crosstalk between plasma cells and synovial fibroblasts Eur. J. Immunol., 2017;0(0):. 2017 [PMID: 28857172] (Bioassay, Human) Bioassay Human
Guanghui Yi Structural and functional attributes of the Interleukin-36 receptor J Biol Chem, 2016;0(0):. 2016 [PMID: 27307043] (Bioassay, Human) Bioassay Human
Saha S, Singh D, Raymond E, Ganesan R, Caviness G, Grimaldi C, Woska J, Mennerich D, Brown S, Mbow M, Kao C Signal Transduction and Intracellular Trafficking by the Interleukin 36 Receptor. J Biol Chem, 2015;290(39):23997-4006. 2015 [PMID: 26269592] (Bioassay, Human) Bioassay Human
van de Veerdonk FL, Stoeckman AK, Wu G, Boeckermann AN, Azam T, Netea MG, Joosten LA, Van der Meer JW, Hao R, Kalabokis V, Dinarello CA IL-38 binds to the IL-36 receptor and has biological effects on immune cells similar to IL-36 receptor antagonist. Proc. Natl. Acad. Sci. U.S.A., 2012;109(8):3001-5. 2012 [PMID: 22315422] (Binding Assay, Human) Binding Assay Human

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Bioinformatics

Gene Symbol IL36RN
Uniprot