Recombinant Human IL-37/IL-1F7 Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When
Recombinant
Human (rh) IL‑18 R alpha /IL‑1 R5 Fc Chimera
(Catalog # 816-LR)
is immobilized at 2 μg/mL (100 μL/well), the concentration of rhIL-37/IL-1F7 Chimera that produces 50% optimal binding response is 20-120 ng/mL.
Source
E. coli-derived human IL-37/IL-1F7 protein Lys27-Asp192, with an N-terminal Met
>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
Dilutions
Binding Activity
Theoretical MW
18.6 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 1975-IL 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 and DTT.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 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-37/IL-1F7 Protein, CF
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). The longest IL-1F7 transcript encodes IL-37b, which 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).
Dinarello, C.A. and P. Bufler (2013) Sem. Immunol. 25:466.
Boraschi, D. et al. (2011) Eur. Cytokine Netw. 22:127.
Ding, V.A. et al. (2016) Med. Oncol. 33:68.
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.
Pan, G. et al. (2000) Cytokine 13:1.
Nold, M.F. et al. (2010) Nat. Immunol. 11:1014.
McNamee, E.N. et al. (2011) Proc. Natl. Acad. Sci. USA 108:16711.
Kumar S. et al. (2002) Cytokine 18:61.
Bufler, P. et al. (2002) Proc. Natl. Acad. Sci. USA 99:13723.
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