Invitrogen™ Mouse DFFB Synthetic Peptide

Caspase-activated DNase (CAD) cleaves chromosomal DNA during apoptosis. Apoptosis which is a cell death process removing toxic and/or useless cells during mammalian development can be induced by a variety of stimuli, including the death factors of the tumor necrosis factor family, or UV irradiation, anticancer drugs, and survival factor deprivation. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units. CAD, which can be activated by caspases, exists as a complex with its inhibitor, inhibitor of CAD (ICAD). ICAD helps correct folding of CAD and remains complexed with CAD to inhibit the DNase activity of CAD. Caspase, which is activated during the apoptotic process, cleaves ICAD, and the CAD released from ICAD enters the nuclei to cleave the chromosomal DNA. Internal as well as external signals can activate caspases and this is under the control of the balance between pro-and anti-apoptotic proteins of the Bcl-2 family, heat shock proteins, and inhibitors of apoptosis proteins (IAPs). Currently, fourteen members of the caspase family have been identified, of which seven mediate apoptosis.