Apoptosis Detection
Apoptosis Assays and Cell Death Reagents
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Fluorescent |
FLICA® Caspase Assay Kits: |
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MitoPT™ Mitochondrial Permeability Transition Assay Kits: FLISP™ Serine Protease Detection Assay Kits: Annexin V-FITC Apoptosis Detection Kit: |
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| In Vivo Apoptosis Assays |
FLIVO® in vivo Apoptosis Assays: injectable inhibitor-based apoptosis tracers with visible and NIR fluorescence for in vivo apoptosis detection and imaging in live animal models |
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| Fluorescent Substrate Assay |
Magic Red™ Caspase 3 & 7 Assay Kits: substrate-based, whole cell assays for real-time visualization of caspase 3 & 7 activation during cellular apoptosis |
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| Live/Dead Assay |
Live/Dead Stains: fluorescent viability staining solutions and live/dead stains for identifying necrosis and membrane-compromised cells |
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| Apoptosis Inducers |
Apoptosis-Inducing Reagents: create positive controls with known apoptosis-inducing chemicals for in vitro apoptosis research |
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Product Catalog: 2013 Fluorescent Probes and Whole Cell Assays Application Guide
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 caspase 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 cellular apoptosis and inflammation. The activation of serine proteases, loss of plasma membrane integrity, and the change in mitochondrial membrane permeability are also common physiological effects of cell death. As such, caspase assays, live/dead stains (live cell impermeant), and mitochondrial permeability assays are useful in the investigation of cellular apoptosis and cell death.
References:
- Slee, E. A., C. Adrain, and S. J. Maritin. (1999) Serial Killers: ordering caspase activation events in apoptosis. Cell Death Differ. 6:1067-1074.
- 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.
- Hengartner, M.O. (2000) The biochemistry of apoptosis. Nature 407:770-816.
- Degterev, A., Boyce, M., and Yuan, J. (2003) A decade of caspases. Oncogene 22:8543-8567.
