The process of apoptosis, or programmed cell death, is fundamental during normal development and homeostasis and aberrant apoptosis has been implicated in a number of human diseases. The cellular machinery involved in the execution of apoptosis includes a family of cysteine proteases termed caspases. Caspases exhibit the rare substrate preference of cleavage C-terminal to aspartate residues, a property shared only by the cytotoxic lymphocyte serine protease, granzyme B. Experimental evidence demonstrates a vital role for caspase activation in the apoptotic pathway, and, as such, caspases are a target for the development of agents that can modulate their activity. This article reviews the members of the caspase family and the role that each contributes to the execution of cell death induced by apoptotic stimuli.