Human IL-37/IL-1F7 Antibody Summary
Lys53-Val206
Accession # Q9NZH6
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of IL-37/IL-1F7 in Human PBMC Monocytes by Flow Cytometry. Human peripheral blood mononuclear cell (PBMC) monocytes either (A) untreated or (B) treated with 250 ng/mL LPS and 3 µM monensin overnight were stained with Mouse Anti-Human IL-37/IL-1F7 Monoclonal Antibody (Catalog # MAB19751, filled histogram) or isotype control antibody (Catalog # MAB0041, open histogram), followed by Phycoerythrin-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # F0102B). To facilitate intracellular staining, cells were fixed with paraformaldehyde and permeabilized with saponin.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: IL-37/IL-1F7
Human Interleukin 1 Family Member 7 (IL-1F7), also named IL-37, FIL-1Z, IL-1H4, and IL-1RP1, belongs to the IL-1 cytokine family. With the exception of IL-18 that maps to human chromosome 11, all other IL-1 family members map to the same cluster on human chromosome 2. Five alternatively spliced transcripts that arise through alternate exon usage have been described. These transcripts encode five different IL-1F7 isoforms (IL-1F7a through e also referred to as isofoms 1 through 5) that have distinct expression profiles. Polymorphism in the protein sequence of IL-1F7 isoforms also exists. Like IL-1 alpha, IL-1 beta and IL-18, all of the IL-1F7 variants lack a typical signal peptide. The longest IL-1F7 transcript, referred to as IL-1F7b or IL-1F7 isoform 1, encodes a 218 amino acid (aa) residues proprotein containing a 45 aa propeptide, which is removed by caspase-1 to generate the 173 aa mature segment. Mature IL-1F7b and other IL-1F7 variants lack potential N-linked glycosylation sites. IL-1F7 shares approximately 21%, 24%, and 30% aa sequence identity with mature IL-1 alpha, IL-1 beta and IL-1ra, respectively. Mouse IL-1F7 has not been reported, but human IL-1F7 is active on mouse cells. IL-1F7b binds to IL-18 R alpha with low affinity but does not exert any IL-18 agonistic or antagonistic effects. IL-1F7b also binds to the IL-18BP to enhance the antagonistic effects of IL-18BP. It has been proposed that IL-1F7b form a trimeric complex with IL-18BP and IL-18 R beta. This complex blocks IL-18 activity by sequestering the signal transducing subunit and preventing it from participating in IL-18 signaling (1‑8).
- Smith, D.E. et al. (2000) J. Biol. Chem. 275:1169.
- Kumar S. et al. (2000) J. Biol. Chem. 275:10308.
- Busfield S.J. et al. (2000) Genomics 66:213.
- Kumar S. et al. (2002) Cytokine 18:61.
- Bufler, P. et al. (2002) Proc. Natl. Acad. Sci. USA 99:13723.
- Gao, W. et al. (2003) J. Immunol. 170:1077.
- Pan, G. et al. (2001) Cytokine 13:1.
- Sims, J.E. et al. (2001) Trends Immunol. 22:533.
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