Recombinant Human IL-18 BPa Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit the IL-18-induced response of KG‑1 human acute myelogenous leukemia cells. The ED50 for this effect is 0.02‑0.12 µg/mL in the presence of 40 ng/mL of recombinant human IL-18.
Source
Mouse myeloma cell line, NS0-derived human IL-18 BPa protein
Human IL-18 Bpa (Thr29-Gly192) Accession # AAD17190
>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
Bioactivity
Theoretical MW
44.2 kDa (monomer). 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
60-80 kDa, reducing conditions
Publications
Read Publications using 119-BP 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 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-18 BPa Fc Chimera Protein, CF
IL18 BPa
IL-18 BPa
IL18BP
IL-18BP
IL18BPa
interleukin 18 binding protein
interleukin-18-binding protein
MC51L-53L-54L homolog gene product
tadekinig-alfa
Background
Interleukin 18 binding protein (IL-18 BP) is a secreted glycoprotein, which functions as an IL-18 antagonist by binding to IL-18 and blocking its biological activity. IL‑18 BP bears no amino acid sequence homology to the membrane-associated IL-18 and IL-1 receptor proteins. The gene for human IL-18 BP has been localized to chromosome 11q13. It encodes for at least four isoforms by alternative splicing. The IL-18 BP isoforms a and c each contain one immunoglobulin (Ig)-like C2-type domain while isoforms b and d lack a complete Ig domain. The complete Ig domain has been shown to be essential to the binding and neutralizing properties of the binding proteins. Two isoforms of mouse IL18 BP (c and d) containing the complete Ig domain have also been isolated and shown to neutralize IL-18 bioactivity. Human and mouse IL-18 BPs share approximately 61% amino acid sequence identity. Several poxviruses also encode proteins with sequence similarity to the human and mouse IL-18 BP. Viral IL-18 BPs have been shown to bind and inhibit IL-18 responses and may be involved in modulating host immune responses. The expression of IL-18 BP is markedly up-regulated by IFN-gamma , suggesting that IL-18 activity is modulated by a negative feedback mechanism mediated by IL-18 BP.
Mühl, H. et al. (2000) Biochem. Biophys. Res. Commun. 267:960.
Kim, S-H. et al. (2000) Proc. Nat. Acad. Sci. USA 97:1190.
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