Recombinant Human IL-36Ra/IL-1F5 (Catalog # 1275-IL/CF) inhibits Recombinant Human IL-36 beta/IL-1F8 (Catalog # 6834-ILB) induced IL-8 secretion by A431 human epithelial carcinoma cells. The ED50 for this effect is ...read more
Recombinant Human IL-36Ra/IL-1F5 Protein, CF 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
>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
Dilutions
Bioactivity
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/CF in the following applications:
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.
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, CF
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).
Smith, D. E. et al. (2000) J. Biol. Chem. 275:1169.
Kumar, S. et al. (2000) J. Biol. Chem. 275:10308.
Mulero, J.J. et al. (1999) Biochem. Biophys. Res. Commun. 263:702.
Nicklin, M.J.H. et al. (2002) Genomics. 79:718.
Barton, J.L. et al. (2000) Eur. J. Immunol. 30:3299.
Dinarello, C. et al. (2010) Nat. Immunol. 11:973.
Dunn, E. et al. (2001) Trends Immunol. 22:533.
Debets, R. et al. (2001) J. Immunol. 167:1440.
Towne, J.E. et al. (2004) J. Biol. Chem. 279:13677.
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