The caspase family includes cysteine peptidases that play key roles in apoptosis and pyroptosis, processes of programmed cell death. There are 14 caspases discovered to date, although only a subset directly function in apoptosis in humans. Caspases 2, 3, 6, 7, 8, 9, and 10 are active in apoptosis and caspases 1, 4, 5, and 12 work in pyroptosis. First produced as inactive proenzymes, caspases become activated upon cleavage. With the proper stimuli initiator caspases, such as caspase 9, proceed to activate executioner caspases 3, 6 and 7. Caspases cleave proteins at aspartic acid sites mediated by a cysteine in the enzyme active site. ELISA kits that detect and quantify members of the caspase family may be valuable in studying the processes of apoptosis, cell proliferation and cancer-related pathways.