The Alzheimer Amyloid Precursor Protein (APP) is a transmembrane protein whose abnormal processing is associated with the pathogenesis of Alzheimer’s disease. APP695 lacking the protease inhibitor domain is the predominant form in neuronal tissues. APP695 is cleaved by caspases into the 664-residue amino (N)-terminal fragment that lacks the carboxyl C-terminal 31-residues (APPΔC31) and the 31-residues C-terminal fragment (APP-C31). Both fragments might be potent inducers of neuronal apoptosis. An antibody (named ACT1) against the N-terminus of caspase 3-generated APP C-terminal 31 aa of human APP695 (APP-C31) was raised in rabbit.
Data Link: Swiss-Prot P05067
1) Western blotting (dilution: 1/3,000-1/1,000)
2) Immunocytechemistry (dilution: 1/1,000-1/500)
These applications were confirmed in the laboratory of Prof. K, Yoshikawa of Osaka University.
< Immunocytochemistry >
Generation of the caspase-cleaved fragments in NT2 neurons (neurally differentiated human NT2 embryonic carcinoma cells) overexpressing wild type APP (ref.3).
NT2 neurons were fixed 72 h after infection with adenovirus vector expressing wild-type APP and stained for the N-terminus of APP (P2-1, mouse monoclonal antibody), chromosomal DNA (Hoechst), the C-terminus of APPΔC31 (SAC) or the N-terminus of APP-C31 (ACT1). Most of wild-type APP-accumulating neurons with shrunken and fragmented nuclei contain SAC- and ACT1-immunoreactivities (arrows), but non-neuronal cells are hardly labeled with SAC and ACT1 (arrowheads).
This antibody was used in ref.3..
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