Interleukin-1 beta (rhIL-1ß) is a proinflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL-1 alpha and IL-1 beta binds to the same receptor and has similar if not identical biological properties. These cytokines have a broad range of activities including, stimulation of thymocyte proliferation, by inducing IL-2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1 beta is a secreted cytokine, IL-1 alpha is predominantly a cell-associated cytokine.
Recombinant human Interleukin-1 beta (rhIL-1ß) produced in E. coli is a single non-glycosylated polypeptide chain containing 153 amino acids. A fully biologically active molecule, rhIL-1ß has a molecular mass of 17.3kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.