|IL‑1 beta /IL‑1F2 in Rat Splenocytes. IL‑1 beta /IL‑1F2 was detected in immersion fixed rat splenocytes treated with PMA and calcium ionomycin using Goat Anti-Rat IL‑1 beta /IL‑1F2 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF501) at 15 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Streptavidin (red; Catalog # NL999) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Non-adherent Cells.|
IL-1 is a name that designates two pleiotropic cytokines, IL-1 alpha (IL-1F1) and IL-1 beta (IL-1F2), which are the products of distinct genes. IL-1 alpha and IL-1 beta are structurally related polypeptides that share approximately 26% amino acid (aa) identity in rat. Both proteins are produced by a wide variety of cells in response to inflammatory agents, infections, or microbial endotoxins. While IL-1 alpha and IL-1 beta are regulated independently, they bind to the same receptor and exert identical biological effects. IL‑1 RI binds directly to IL-1 alpha or IL-1 beta and then associates with IL-1 R accessory protein (IL-1 R3/IL-1 R AcP) to form a high-affinity receptor complex that is competent for signal transduction. IL-1 RII has high affinity for IL-1 beta but functions as a decoy receptor and negative regulator of IL-1 beta activity. IL-1ra functions as a competitive antagonist by preventing IL-1 alpha and IL-1 beta from interacting with IL-1 RI (1-4). The rat IL-1 beta cDNA encodes a 268 aa precursor. A 116 aa propeptide is cleaved intracellularly by the cysteine protease IL-1 beta -converting enzyme (Caspase-1/ICE) to generate the active cytokine (5, 6). The 17 kDa mature rat IL-1 beta shares 90% aa sequence identity with cotton rat and mouse and 65-77% with canine, equine, feline, human, porcine, and rhesus IL-1 beta.
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