Cleaved Caspase 3 Apoptosis
Cleaved Caspase-3 (Asp175) Western Detection Kit offers an efficient way of detecting caspase-3 processing and activation by Western blotting.
Cleaved caspase 3 apoptosis. The sequential cleaving and activation of these proteins is crucial to the execution stage of preprogrammed cellular death. After this process, the caspase 3 protein is cleaved and broken down itself by caspase 8 and 10, as well as any inactive caspase 9 proteins that have yet to be cleaved themselves. This caspase is responsible for the majority of proteolysis during apoptosis, and detection of cleaved caspase-3 is therefore considered a reliable marker for cells that are dying, or have died by apoptosis.
This protocol outlines the quantification of apoptosis by flow cytometric detection of cleaved caspase-3. The role of caspase 3 in apoptosis is to cleave and activate caspases 6, 7 and 9 in order to break down the apoptotic cells before removal. Among them, caspase-3 is a frequently activated death protease, catalyzing the specific cleavage of many key cellular proteins.
Analysis Of Apoptotic Pathways By Western Blot
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