Recombinant Human IL-36 beta/IL-1F8 Protein


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Product Details

Reactivity HuSpecies Glossary
Applications Binding Activity

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Recombinant Human IL-36 beta/IL-1F8 Protein Summary

Additional Information
A New rh IL-36b is Now Available! The new truncated protein is 40-fold more active!
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized recombinant human IL-36 beta at 1 µg/mL (100 µL/well) can bind recombinant human IL-1 Rrp2 Fc Chimera (Catalog # 872-RP) with a linear range of 0.15-5 µg/mL.
E. coli-derived human IL-36 beta/IL-1F8 protein
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


Theoretical MW
17.7 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.
Read Publications using
1099-IL in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.


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

Alternate Names for Recombinant Human IL-36 beta/IL-1F8 Protein

  • family of interleukin 1-eta
  • FIL1 eta
  • FIL1
  • FIL1-(ETA)
  • FIL1H
  • FILI-(ETA)
  • IL-1 eta
  • IL1-ETA
  • IL1F8 (Canonical product IL-1F8a)
  • IL-1F8 (FIL1-eta)
  • IL1F8
  • IL-1F8
  • IL1H2
  • IL-1H2
  • IL36 beta
  • IL-36 beta
  • IL36B
  • interleukin 1 family, member 8 (eta)
  • interleukin 1, eta
  • Interleukin 36, Beta
  • Interleukin-1 eta
  • interleukin-1 family member 8
  • Interleukin-1 homolog 2
  • Interleukin-1 Superfamily e
  • Interleukin-36 Beta


Human interleukin‑36 beta [IL‑36 beta ; previously IL‑1F8 and also named FIL‑1 eta  (eta) and IL‑1H2] is a member of the IL‑1 family of proteins (1 ‑ 3, 6). IL‑1 family members include IL‑1 beta, IL‑1 alpha, IL‑1ra, IL‑18, IL‑36Ra/IL‑1F5, IL‑36 alpha /IL‑1F6, IL‑37/IL‑1F7, IL‑36 gamma /IL‑1F9 and IL‑1F10 (4, 6). All family members show a 12 beta ‑stranded beta ‑trefoil configuration, and are believed to have arisen from a common ancestral gene that has undergone multiple duplications (4). Two alternatively spliced transcript variants encode distinct (164 or 157 residues) protein isoforms that differ in their C‑terminal 70 amino acid (aa) residues have been reported (3). IL‑36 beta /IL‑1F8 isoform 2 is synthesized as a 157 aa protein that contains no signal sequence and no prosegment (1 ‑ 2). Unlike IL‑36 beta /IL‑1F8 isoform 1 which lacks potential N‑linked glycosylation sites, isoform 2 contains one potential N‑linked glycosylation site in its unique C‑terminus. IL‑36 beta /IL‑1F8 is reported to be actively secreted (1). Human IL‑36 beta /IL‑1F8 isoform 2 shares 61% aa identity with mouse IL‑1 ra, a 183 aa form of IL‑36 beta /IL‑1F8. Within the IL‑1 family, IL‑36 beta /IL‑1F8 shares 30%, 32%, 37%, 46%, 34%, 45% and 28% aa sequence identity with IL‑1 ra, IL‑1 beta, IL‑36Ra/IL‑1F5, IL‑36 alpha /IL‑1F6, IL‑37/IL‑1F7, IL‑36 gamma /IL‑1F9 and IL‑1F10, respectively. Cells reported to express IL‑36 beta /IL‑1F8 include resting and activated monocytes and B cells (1, 4). The receptor for IL‑36 beta /IL‑1F8 is reported to be a combination of IL‑1 Rrp2 and IL‑1 RAcP (5). Recombinant IL‑36 beta /IL‑1F8, along with IL‑36 alpha /IL‑1F6 and IL‑36 gamma /IL‑1F9, has been shown to activate the pathway involving NF‑ kappa B and MAPK in an IL‑1 Rrp2 dependent manner.

  1. Smith, D.E. et al. (2000) J. Biol. Chem. 275:1169.
  2. Kumar, S. et al. (2000) J. Biol. Chem. 275:10308.
  3. Nicklin, M.J.H. et al. (2002) Genomics 79:718.
  4. Dunn, E. et al. (2001) Trends Immunol. 22:533.
  5. Towne, J.E. et al. (2004) J. Biol. Chem. 279:13677.
  6. Dinarello, C. et al. (2010) Nat. Immunol. 11:973.

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Gene Symbol IL36B