Recombinant Human IL-37/IL-1F7 Protein

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Recombinant HumanIL-37/IL-1F7(Catalog # 9225-IL) inhibits LPS-stimulated IL-8 secretion by HK-2 human kidneyepithelial cells. The ED50 for this effect is 0.25-1.25 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human IL-37/IL-1F7 Protein Summary

Details of Functionality
Measured by its ability to inhibit LPS-stimulated IL-8 secretion by HK-2 human kidney epithelial cells. The ED50 for this effect is 0.25-1.25 μg/mL.
Source
E. coli-derived human IL-37/IL-1F7 protein
Ser2-Asp192
Accession #
N-terminal Sequence
Ser2
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
21 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.
SDS-PAGE
22 kDa, reducing conditions

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 and DTT with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human IL-37/IL-1F7 Protein

  • FIL1 zeta
  • FIL1
  • FIL1(ZETA)
  • FIL1ZFIL1 zeta
  • IL-1F7
  • IL-1F7IL-1 zeta
  • IL1H4IL1F7 (canonical product IL-1F7b)
  • IL-1H4IL-1F7b (IL-1H4, IL-1H, IL-1RP1)
  • IL-1RP1IL-1X protein
  • IL1RP1interleukin 1 family member 7
  • IL-1X
  • IL37
  • IL-37
  • interleukin 1 family, member 7 (zeta)
  • interleukin 1, zeta
  • interleukin-1 family member 7
  • Interleukin-1 homolog 4
  • interleukin-1 superfamily z
  • Interleukin-1 zeta
  • Interleukin-1-related protein

Background

Human Interleukin-1 family member 7 (IL-1F7), also named FIL-1 zeta, IL-37, IL-1H4, IL-1HL and IL-1RP1, is an anti-inflammatory member of the IL-1 cytokine family (1-3). Alternative splicing generates multiple isoforms (IL-37a through e) with deletions in the N-terminal region of the molecule (4-7). IL-37b shares approximately 21%, 24%, and 30% aa sequence identity with mature IL-1 alpha, IL-1 beta, and IL-1ra, respectively. Mouse IL-37 has not been reported, but human IL-37b is active on mouse cells. Like IL-1 alpha, IL-1 beta and IL-18, all of the IL-37 variants lack a typical signal peptide. IL-37b is up-regulated by inflammatory stimuli in peripheral blood mononuclear cells (8). Experimental over-expression of IL-37b in vivo limits the inflammatory response and protects mice from colitis and LPS-induced shock (8, 9). Both unprocessed and mature IL-37b can form homodimers in solution (8, 10). Although IL-37b will bind to IL-18 R alpha with low affinity, this has no effect on IL‑18 receptor activity (7, 10, 11). Alternatively, IL-37b will also bind to IL-18 BP, generating a complex that interacts with IL-18 R beta. This has the effect of attenuating IL‑18 activity via the IL-18 receptor (11). IL-37b can also function intracellularly. Following LPS-induced cleavage of its propeptide, IL-37b associates with Smad3 and translocates to the nucleus. This results in a reduction of pro-inflammatory cytokine secretion (12).
  1. Dinarello, C.A. and P. Bufler (2013) Sem. Immunol. 25:466.
  2. Boraschi, D. et al. (2011) Eur. Cytokine Netw. 22:127.
  3. Ding, V.A. et al. (2016) Med. Oncol. 33:68.
  4. Smith, D.E. et al. (2000) J. Biol Chem 275:1169.
  5. Kumar S. et al. (2000) J. Biol Chem 275:10308.
  6. Busfield S.J. et al. (2000) Genomics 66:213.
  7. Pan, G. et al. (2000) Cytokine 13:1.
  8. Nold, M.F. et al. (2010) Nat. Immunol. 11:1014.
  9. McNamee, E.N. et al. (2011) Proc. Natl. Acad. Sci. USA 108:16711.
  10. Kumar S. et al. (2002) Cytokine 18:61.
  11. Bufler, P. et al. (2002) Proc. Natl. Acad. Sci. USA 99:13723.
  12. Sharma, S. et al. (2008) J. Immunol. 180:5477.

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