Caspase-8 is a member of the aspartate-specific cysteine protease family that is typically synthetized as an inactive zymogen and activated upon an appropriate stimulus. Caspase-8 plays an essential role in apoptotic signal transduction from the death receptor. Recruitment of procaspase-8 into the death signaling complex leads to its dimerization, autoproteolytic cleavage and formation of a highly active heterotetramer. Caspase-8 subsequently activates caspase-3, thereby initiating the proteolytic pathway, and ultimately resulting in the apoptotic disassembly of the cell.1 Additionally, caspase-8 is also essential for various immune processes, such as lymphocyte activation, inflammasome regulation and cytokine production