IL1B Mouse, His Active

IL-1β is a member of the interleukin-1 family, which includes IL-1α and IL-1 receptor antagonist (IL-1Ra). The mature IL-1β protein consists of 153 amino acids and has a molecular weight of approximately 17.5 kDa. It binds to the IL-1 receptor type I (IL-1R1) on target cells, initiating a signaling cascade that leads to the activation of nuclear factor-kappa B (NF-κB) and mitogen-activated protein kinases (MAPKs). These signaling pathways result in the production of other pro-inflammatory cytokines, chemokines, and adhesion molecules, amplifying the inflammatory response.

Recombinant human IL-1β is produced using various expression systems, including Escherichia coli and mammalian cells. The recombinant protein is often tagged with a His (histidine) tag to facilitate purification and detection. The His tag is a short sequence of histidine residues that binds to nickel ions, allowing the protein to be purified using nickel-affinity chromatography.

Recombinant IL-1β is widely used in research to study its role in inflammation and immune responses. It is also used in various assays, including enzyme-linked immunosorbent assays (ELISAs), functional assays, and cell culture experiments. The bioactive form of recombinant IL-1β is essential for these studies, as it retains the ability to bind to IL-1R1 and activate downstream signaling pathways.

IL-1β is a key mediator of the inflammatory response and has been implicated in various diseases, including rheumatoid arthritis, inflammatory bowel disease, and sepsis. It induces the production of prostaglandins, nitric oxide, and reactive oxygen species, which contribute to the inflammatory process. IL-1β also promotes the differentiation of T-helper 17 (Th17) cells, which play a role in autoimmune diseases.