Anti-IL-18, clone IL18/7781

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. Four structurally related IL-1 receptor ligands have been described. These include three agonists designated IL-1Alpha, IL-1beta and IL-1gamma/IL-18 and a specific receptor antagonist, IL-1RAlpha. IL-1Alpha and IL-1beta play critical roles in the regulation of the immune response and inflammation, serving as activators of T and B lymphocytes and NK (natural killer) cells. IL-18 (also referred to as IL-1gamma) has been shown to augment the secretion of IFN-gamma from T lymphocytes and increase NK cell activity in spleen cells. IL-18 exhibits 19% and 12% identity with IL-1Alpha and IL-1beta respectively over the 12 beta-strands of the beta-trefoil fold domain, which is a signature feature of the IL-1 family. The unusual leader sequence of IL-18 may be analogous to the IL-1beta pro-domain which must be cleaved by the serine protease ICE for optimal secretion and biological activity. Originally described as IGIF (IFN-gamma-inducing factor), IL-18 is induced by mouse liver subsequent to challenge with lipopolysaccharide (LPS). Protein function: Pro-inflammatory cytokine primarily involved in epithelial barrier repair, polarized T-helper 1 (Th1) cell and natural killer (NK) cell immune responses (PubMed:10653850). Upon binding to IL18R1 and IL18RAP, forms a signaling ternary complex which activates NF-kappa-B, triggering synthesis of inflammatory mediators (PubMed:14528293, PubMed:25500532). Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells and natural killer (NK) cells (PubMed:10653850). Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33883744). [The UniProt Consortium]