Reactivity | Pm-CmSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
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 0.015-0.075 μg/mL |
Source | Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey IL-18 BPa protein Thr28-Pro207, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Thr28 |
Structure / Form | Monomer |
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. |
Dilutions |
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Theoretical MW | 20 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 | 54-60 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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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 500 μg/mL in PBS. |
Cynomolgus Interleukin 18 binding protein (IL-18 BP) is a 20 kDa secreted glycoprotein, which functions as an IL-18 antagonist by binding to IL-18 and blocking its biological activity (1). IL-18 BP bears no amino acid sequence homology to the membrane-associated IL-18 and IL-1 receptor proteins. Human IL-18BP encodes for at least four isoforms by alternative splicing. The IL-18 BP isoform a and c each contains one immunoglobulin (Ig)-like C2-type domain while isoform 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 (2). Cynomolgus IL-18BPa shares 83% sequence identity with human and 62% with mouse IL-18BPa, respectively. Several poxviruses also encode proteins with sequence similarity to 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 upregulated by IFN-gamma, suggesting that IL-18 activity is modulated by a negative feedback mechanism mediated by IL-18 BP (3).
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