Caspases are a family of proteins that play a critical role in apoptosis.  They belong to a group of enzymes known as cysteine proteases and exist within the cell as inactive pro-caspases.  This family can be divided into three classes: initiator caspases, effector caspases, and cytokine processors.  Initiator caspases (caspase-2, caspase-8, caspase-9, caspase-10) are the first to be activated, which then cleave and activate the effector caspases (caspase-3, caspase-6, caspase-7).  Effector caspases cleave, degrade and activate other protein substrates within the cell, such as cytoskeletal proteins, to trigger apoptosis.  Some caspases (caspase-1, caspase-4, caspase-5, caspase-11, caspase-12, caspase-13, caspase-14) have a specialized role in inflammation and their activation leads to the processing of pro-inflammatory cytokines.  The caspase cascade can be activated by numerous mechanisms, including delivery of granzyme B, apoptosome formation and death cell receptors.  Caspase activation leads to characteristic morphological changes of the cell, such as shrinkage, DNA fragmentation, plasma membrane blebbing and chromatin condensation.

All Caspase Antibodies, Lysates, Proteins, and RNAi

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