Caspases are a family of cysteine-aspartic proteases that are key players in programmed cell death, including apoptosis and pyroptosis.There are 11 established functional protein members in humans: Caspases 2, 3, 6, 7, 8, 9, and 10 play roles in apoptosis while caspases 1, 4, 5, and 12 function in pyroptosis. Caspases are first synthesized as inactive zymogens and are activated by cleavage. Initiator caspases, such as Caspase 9, can self-activate with the right signal and proceed to activate executioner caspases 3, 6 and 7. The downstream proteolysis of cellular components results from cleavage of aspartic acid residues mediated cysteine in the active site. Antibodies targeting members of the caspase family may prove useful in investigating apoptosis, cell proliferation and cancer.