Caspases are a family of cysteine proteases which play essential roles in apoptosis. Among them, Caspase 3 is a frequently activated death protease, catalyzing the specific cleavage of many key cellular proteins. Caspase 3 is synthesized as an inactive 32 kDa pro-enzyme which undergo proteolytic processing in response to apoptotic stimulation to produce the active form which consists of the p20/p17, and p12 subunits. Caspase 3 is the predominant caspase involved in the cleavage of Alzheimer amyloid precursor protein (APP), which is associated with neuronal death in Alzheimer ‘s disease. An antibody (named ACP3) against activated caspase 3 was raised in rabbit. This antibody recognizes the active form of human caspase 3, p20/p17 subunit but does not recognize the proenzyme p32.
Data Link: Swiss-Prot P42574
1) Western blotting (dilution: 1/3,000-1/1,000)
2) Immunocytochemistry (dilution: 1/1,000-1/500)
Immunocytochemistry for APP, chromosomal DNA, and activated caspase 3 subunits : Caspase 3 activation in neurons accumulating wild-type APP (ref.3).
NT2 neurons (neurally differentiated human NT2 embryonic carcinoma cells) were infected with adenovirus vector expressing β-galactosidase (upper panel) or APP (lower panel), fixed 48 h later, and triply stained for the N-terminus of APP (with antibody P2-1) or β-gal (with antibody against β-gal), chromosomal DNA (Hoechst), and activated caspase 3 subunits (with antibody ACP3). Some neurons accumulating APP are strongly immunostained with ACP3 (arrows), whereas neurons accumulating β-gal are hardly labeled (arrowheads). β-gal APP Hoechst ACP3 β-gal or APP.
This antibody was used in ref.3 and 4.
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Anti Activated Caspase 3