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A Further Step in Understanding Apoptosis,,, Direct Detection of PARP Cleavage

Detection of early apoptotic events has become quite relevant since many studies have demonstrated that abnormalities in cell death regulation cause a variety of diseases and pathological conditions accompanied either by cell accumulation (e.g., cancer) or by cell loss (e.g., Alzheimers dementia).

One of the key initiation elements of the apoptotic pathway is the activation of caspases (cysteinyl-aspartic acid proteases) followed by cleavage of the caspase substrates [1]. The 113-kDa poly(ADP-ribose) polymerase 1 (PARP-1), which is normally involved in DNA repair, DNA stability, and other cellular events, is cleaved by members of the caspase family during early apoptosis. The zincdependent eukaryotic DNA-binding protein PARP-1 specifically recognizes DNA strand breaks produced by various genotoxic agents. Detection of a 89-kDa or 24-kDa caspase cleavage fragment of PARP-1 was shown to be a hallmark of apoptosis [2]. In contrast to measuring active caspase 3, which is degraded during apoptosis via the ubiquitin/proteosome pathway, measuring PARP-1 cleavage might allow sustained signal detection even in late stages of apoptosis.

Product Description

With the anti-PARP Caspase Cleavage Product Antibody you will specifically detect only the small apoptotic PARP-1 cleavage fragment, but not the full-length protein, in samples of human, mouse, or rat origin. The fluorescein- conjugated monoclonal antibody (clone PAR-16) enables direct detection of this early apoptosis marker.

Furthermore it provides a tool for apoptotic-pathway analysis (in situ) at the stage of caspase activity. It can be
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