Caspase Detection Assays

ImmunoChemistry Technologies offers a wide range of caspase detection products:
FLICA^®Caspase Detection Kits are inhibitor-based assays containing fluorescent caspase inhibitor probes for detecting caspase 1, 2, 3, 6, 8, 9, 10, 13 or poly caspases.
Magic Red™ Caspase 3&7 Assay Kits offer a no wash, substrate-based assay for real-time visualization of caspase 3&7 activation.
FLIVO™ in vivo Apoptosis Kits allow for the in vivo detection of apoptotic cells and tissues by labeling active caspases with our non-toxic apoptosis probes.

Apoptosis is an evolutionarily conserved form of cell suicide mediated by a cascade of proteolytic enzymes known as cysteine proteases, or caspases. Pro-apoptotic signals activate the enzymatic cascade resulting in the cleavage of protein substrates, leading to the disassembly of the cell (1-4). Caspases have been identified in organisms ranging from C. elegans to humans. Members of the mammalian caspase family of cysteinyl aspartate-specific proteases play distinct roles in apoptosis and inflammation. Caspases are categorized in two groups: the initiators (caspases 8, 9, and 10) and the effector caspases (caspases 1, 2, 3, 4, 6, 7, 12, and 13). The initiator caspases 8 and 10 are also referred to as the extrinsic apoptosis pathway that originates upon activation of cell surface death receptors. Caspases 8 and 10 are monomers that bind to death receptor proteins through their death effector domain (DED) structure. Caspase 9 is also called the intrinsic pathway that results from the mitochondrial release of cytochrome c. The initiator caspase 9 monomer binds other proteins through their caspase activation and recruitment domain (CARD). The initiator caspase-protein interaction results in dimerization of the initiator caspases that leads to their activation. These activated initiator caspases then cleave the effector pro-caspases at specific aspartic acid residues to yield large (20 kDa) and small (10 kDa) subunits that then assemble into the heterotetrameric, catalytically active form of the caspase effector enzymes (5, 6).

References:

1. Slee, E. A., C. Adrain, and S. J. Maritin. (1999) Serial Killers: ordering caspase activation events in apoptosis. Cell Death Differ. 6:1067-1074.
2. Earnshaw, W.C., Martins, L.M., and Kaufmann, S.H. (1999) Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Ann. Rev. Biochem. 68:383-424.
3. Hengartner, M.O. (2000) The biochemistry of apoptosis. Nature 407:770-816.
4. Degterev, A., Boyce, M., and Yuan, J. (2003) A decade of caspases. Oncogene 22:8543-8567.
5. Nicholson, D.W. (1999) Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6:1028-1042.
6. Thornberry, N.A., and Lazebnik, Y. (1998) Caspases: enemies within. Science 281:1312-1316.