In the presence of Recombinant Mouse IL‑12 (0.1 ng/mL, Catalog # 419‑ML), Recombinant Rat IL‑18/IL‑1F4 (Catalog # 521‑RL) stimulates IFN‑ gamma secretion in activated mouse T cells in a dose-dependent ...read more
E. coli-derived recombinant rat IL‑18/IL-1F4 His37-Ser194 Accession # P97636
Detects rat IL‑18/IL-1F4 in direct ELISAs and Western blots. In Western blots, approximately 35% cross-reactivity with recombinant mouse IL‑18 is observed and approximately 10% cross-reactivity with recombinant human IL‑18 is observed.
Immunogen affinity purified
<0.10 EU per 1 μg of the antibody by the LAL method.
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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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Immunogen affinity purified
Reconstitute at 0.2 mg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for IL-18/IL-1F4 Antibody
Interferon gamma-inducing factor
interleukin 18 (interferon-gamma-inducing factor)
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). Rat IL-18 is synthesized as a 24 kDa proprotein that contains a 36 amino acid (aa) propeptide and a 158 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 rat IL-18 shares 91% aa sequence identity with mouse IL-18 and 60-64% aa sequence identity with human, canine, feline, porcine, and rhesus macaque 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, 10-12). 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).
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