Caspase-3
Caspase-3 (CASP3, also known as CPP32, CPP32B, Yama or apopain) is a cysteine-aspartic acid protease and a major effector caspase in the execution phase of apoptosis. Once activated by initiator caspases, it cleaves a wide range of cellular substrates. Browse Assay Genie's current range of Caspase-3 research reagents below, or read on for the biology behind the target.
Caspase-3 is a thiol protease that acts as a major effector caspase in the execution phase of apoptosis. It is itself processed and activated by the initiator caspases CASP8, CASP9 and CASP10. Once active, it catalyses cleavage of many proteins. At the onset of apoptosis it cleaves poly(ADP-ribose) polymerase PARP1 at the 216-Asp-|-Gly-217 bond, a cleavage widely used to follow apoptotic progression. It also cleaves and activates sterol regulatory element binding proteins (SREBPs) and the caspases CASP6, CASP7 and CASP9, and it cleaves and inactivates interleukin-18.
Beyond classical apoptosis, caspase-3 has a broad substrate range. It cleaves DSG2 and JUP, which reduces cell-cell adhesion at desmosome junctions, and it cleaves XRCC4 and the scramblase proteins XKR4, XKR8 and XKR9, promoting phosphatidylserine exposure on the apoptotic cell surface. It cleaves and inhibits AKT1 under oxidative stress, and during virus-induced apoptosis it cleaves the antiviral proteins CGAS, IRF3 and MAVS, limiting type I interferon production. It also activates gasdermin-E (GSDME) in pyroptosis, cleaves BIRC6 after DIABLO/SMAC inhibits BIRC6-caspase binding, and takes part in huntingtin cleavage. In neurons it cleaves RET to trigger cell adhesion in sympathetic neurons and contributes to axon pruning in brain development.
The CASP3 gene encodes a protein of the peptidase C14A family, and is listed by HGNC in the caspase gene group. Mouse and rat both have a Casp3 ortholog. Caspase-3 is the predominant caspase in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. Earlier names include caspase 3, apoptosis-related cysteine protease.
Caspase-3 is a central executioner of apoptosis, cleaving PARP1 and activating other caspases, so it is a core readout of cell death pathways.
It is the predominant caspase cleaving amyloid-beta precursor protein linked to neuronal death in Alzheimer's disease, and it contributes to axon pruning.
Caspase-3 cleaves and activates gasdermin-E, connecting apoptotic signalling with pyroptosis.
By cleaving CGAS, IRF3 and MAVS during virus-induced apoptosis, caspase-3 restrains type I interferon production and cytokine overproduction.
Caspase-3 is an effector protease that executes apoptosis. After activation by CASP8, CASP9 or CASP10, it cleaves many substrates, including PARP1, SREBPs, and the caspases CASP6, CASP7 and CASP9. It also has roles in pyroptosis, phosphatidylserine exposure and loss of cell-cell adhesion.
The CASP3 gene product is also called CPP32, CPP32B, Yama and apopain. Earlier HGNC names were caspase 3, apoptosis-related cysteine protease, and caspase 3, apoptosis-related cysteine peptidase. The enzyme is classed as EC 3.4.22.56 within the peptidase C14A family.
Mouse and rat each have a Casp3 ortholog. Caspase-3 is the predominant caspase cleaving amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease, and it is involved in huntingtin cleavage. Check the datasheet of any product for its validated reactivity.
Other caspase family members, including the initiator caspases that activate caspase-3 and related apoptosis targets.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P42574; product specifications from Assay Genie datasheets.