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Interleukin 1 beta (IL-1β) is synthesized as an inactive precursor protein or pro-IL-1β. This precursor is cleaved intracellularly by Caspase 1 (IL-1β convertase) to form the active form of the protein that is later secreted (Allan et al.). IL-1β binds to IL-1 receptor and activates intracellular signaling via the MAPK or NF-kB pathway. IL-1β is released by monocytes, tissue macrophages, and dendritic cells in response to infection or injury and induces expression of acute-phase proteins. It also promotes the infiltration of inflammatory and immunocompetent cells from the circulation into the extravascular space and affected tissues, by stimulating the expression of adhesion molecules on endothelial cells. IL-1β also affects other immune cells; for example, it co-stimulates T cell functions together with antigen or mitogen. It also stimulates Th17 differentiation and B cell proliferation in an IL-6-dependent manner. This product is animal component-free.
(A) The biological activity of Human Recombinant IL-1 beta, ACF was tested by its ability to promote the proliferation of D10S cells. Cell
proliferation was measured after 66 hours of culture using a fluorometric assay method. The EC50 is defined as the effective
concentration of the cytokine at which cell proliferation is at 50% of maximum. The EC50 in the example above is 0.87 pg/mL.
(B) 1 μg of Human Recombinant IL-1 beta, ACF was resolved with SDS-PAGE under reducing (+) and non-reducing (-) conditions and
visualized by Coomassie Blue staining.
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