Recombinant Rhesus Macaque IL-18/IL-1F4 Protein Summary
Product Specifications
Tyr37-Asp193
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
2548-RM
| Formulation | Lyophilized from a 0.2 μm filtered solution in Tris, NaCl, EDTA, TCEP and PEG 8000 with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 25 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
2548-RM/CF
| Formulation | Supplied as a 0.2 μm filtered solution in Tris, NaCl, EDTA, TCEP and PEG 8000. |
| Reconstitution | 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. |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Scientific Data
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Recombinant Rhesus Macaque IL-18/IL-1F4 (Catalog # 2548-RM) induces 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.
Reconstitution Calculator
Background: IL-18/IL-1F4
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.
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- 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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