Inflammasomes are protein complexes induced by diverse inflammatory stimuli. Innate immune cells respond to pathogens and other danger signals with inflammasome formation and conversion of procaspase-1 zymogen into catalytically active caspase-1. Caspase-1 activation results in: 1) the processing and release of cytokines IL-1β and IL-18 and 2) pyroptosis, an immunogenic form of cell death.

The Caspase-Glo® 1 Inflammasome Assay provides a luminogenic caspase-1 substrate, Z-WEHD-aminoluciferin, in a lytic reagent optimized for caspase-1 activity and luciferase activity. A single addition of this reagent results in cell lysis, substrate cleavage by caspase-1 and generation of light by a proprietary, thermostable, recombinant luciferase (Ultra-Glo™ Recombinant Luciferase). The coupled-enzyme system reaches a steady-state between caspase cleavage of the substrate and luciferase conversion of aminoluciferin. These simultaneous reactions generate a stable luminescent signal, which is proportional to caspase activity. Inclusion of the proteasome inhibitor MG-132 in the reagent eliminates nonspecific proteasome-mediated cleavage of the substrate, enabling sensitive measurement of caspase-1 activity.