Cell death via apoptosis is a key cellular function triggered by the cell death receptor family and their ligands which signal through downstream adaptor molecules and the caspase protease family. Among the subclass of initiator caspases that include subtypes -2, -8 and -9, caspase 9 is expressed in a variety of human tissues. It is a key component in cell death in response to a wide range of activators such as TNFalpha, TRAIL, anti-CD95, FADD, TRADD, granzyme B, and CPP32. Activated caspase 9 primary signaling occurs through caspase 3, which it cleaves and activates. The Caspase 9 antibody was used by Krajewski’s group to characterize caspase 9 mitochondrial release during cytochrome c-dependent apoptosis and ischemia in their neuronal cell culture models1. Immunoblot studies with the Caspase 9 antibody allowed NIH researchers to dissect the complex signaling machinery downstream of cytochrome C, specifically that involving caspase 9 and Bax2. Their data indicates that the association between apoptotic protease activating factor-1 (Apaf-1) and cytochrome C directly influences cell survival.
Western Blot: Caspase 9 Antibody
Cowan et al employed the Caspase 9 antibody to classify in vivo activation of caspases 9 and 3 in olfactory receptor neurons (ORNs) and found that caspase 3 is required for normal bulb development as well as mature differentiation through targeted apoptosis3. Further neurological studies with Caspase 9 antibody in the autosomal dominant progressive disorder Huntington’s disease (HD) helped define caspases 2, 6, and 7 downstream pathways as those responsible for selective neuronal death4. Herold’s group used their characterization studies with Caspase 9 antibody to validate their preserved rat inguinal fat flap system as a permanent extracorporeal perfusion bioreactor system for examining fat cell death5.
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