Recombinant Rhesus Macaque IL-18/IL-1F4 Protein, CF Summary
Details of Functionality |
Measured by its ability to induce IFN-gamma secretion by KG‑1 human acute myelogenous leukemia cells in the presence of TNF-alpha . The ED50 for this effect is 1-4 ng/mL in the presence of 20 ng/mL recombinant human TNF-alpha . |
Source |
E. coli-derived rhesus macaque IL-18/IL-1F4 protein Tyr37-Asp193 |
Accession # |
|
N-terminal Sequence |
Tyr37 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note |
<1.0 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
18.2 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. |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 6 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after opening.
|
Buffer |
Supplied as a 0.2 μm filtered solution in Tris, NaCl, EDTA, TCEP and PEG 8000. |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions |
It is recommended that sterile PBS be added to the vial to prepare a working stock solution of no less than 100 μg/mL. The carrier-free protein should be used immediately upon reconstitution to avoid losses in activity due to non-specific binding to the inside surface of the vial. For long term storage as a dilute solution, a carrier protein (e.g. 0.1% HSA or BSA) should be added to the vial. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Rhesus Macaque IL-18/IL-1F4 Protein, CF
Background
Interleukin-18 (IL-18), also known as IL-1F4 and IFN-gamma inducing factor (IGIF), is a member of the IL-1 family of cytokines and is a key molecule in the innate immune response (1). Rhesus IL-18 is synthesized as a 24 kDa proprotein that contains a 36 amino acid (aa) propeptide and a 157 aa mature region (2). Under inflammatory conditions, the propeptide is cleaved by Caspase-1 in the cytoplasm to liberate the mature nonglycosylated 18 kDa monomeric IL-18 (3, 4). Mature rhesus IL-18 shares 96% aa sequence identity with human IL-18 and 60% - 76% with mouse, rat, canine, feline, and porcine IL-18. IL-18 is secreted by a variety of cell types including macrophages, dendritic cells, and epithelial cells (1, 5). Circulating mature IL-18 is sequestered by soluble IL-18 binding proteins (IL-18 BP) that inhibit IL-18 bioactivity (6). IL-18 interacts with the widely expressed IL-18 R alpha which then recruits the signaling subunit IL-18 R beta (7, 8). The IL-1 family member IL-1F7 also binds to IL-18 R alpha but does not recruit IL-18 R beta or induce signaling (9). IL-1F7 binds IL-18 BP and enhances its neutralizing effect on IL-18 activity (9). IL-18 synergizes with other cytokines to activate NK, Th1, and Th17 cells and to increase the production of IFN-gamma (1, 5, 10, 11, 12). IL-18 can also promote Th2 cytokine release which reduces the effectiveness of antiviral responses (13, 14). Increased levels of active IL-18 contribute to the severity of autoimmunity and hypertension, while deficiency of IL-18 results in symptoms of metabolic syndrome (1, 5, 15, 16). In cancer, IL-18 stimulates Th1 and NK cells to target tumor cells, but it can also promote angiogenesis, metastasis, and tumor cell immune evasion (11).
- Arend, W.P. et al. (2008) Immunol. Rev. 223:20.
- Giavedoni, L.D. et al. (2001) J. Interferon Cytokine Res. 21:173.
- Ghayur, T. et al. (1997) Nature 386:619.
- Gu, Y. et al. (1997) Science 275:206.
- Boraschi, D. and C.A. Dinarello (2006) Eur. Cytokine Netw. 17:224.
- Novick, D. et al. (1999) Immunity 10:127.
- Torigoe, K. et al. (1997) J. Biol. Chem. 272:25737.
- Born, T.L. et al. (1998) J. Biol. Chem. 273:29445.
- Bufler, P. et al. (2002) Proc. Natl. Acad. Sci. 99:13723.
- Takeda, K. et al. (1998) Immunity 8:383.
- Park, S. et al. (2007) Cell. Mol. Immunol. 4:329.
- Yoshimoto, T. et al. (1998) J. Immunol. 161:3400.
- Hoshino, T. et al. (2001) J. Immunol. 166:7014.
- Iannello, A. et al. (2009) AIDS Rev. 11:115.
- Rabkin, S.W. (2009) Nat. Clin. Pract. Cardiovasc. Med. 6:192.
- Netea, M.G. et al. (2006) Nat. Med. 12:650.
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