Apoptosis Detection Products

Description

Apoptosis, a form of programmed cell death, is among the most highly studied and analyzed processes in cell biology. The components of the core cell-death machinery are integral to cells and widely conserved across species. Caspases, a family of cysteinyl aspartate-specific proteases, are integral components of the cell death machinery and have central roles in the initiation and execution of apoptosis. Caspases are synthesized as inactive pro enzyme precursors (zymogens) of ~30-55 kDa with an N-terminal prodomain of variable length followed by a large subunit (p20) and a small subunit (p10). Caspase activation is a hallmark of apoptotic signaling pathways. Caspases are activated early during apoptosis through proteolytic cleavage at specific asparagine residues by self-proteolysis and/or cleavage by other caspases. The asparagine resides are located within the prodomain, the p10, and p20 subunits. Activation results in the generation of mature active caspases consisting of the heterotetramer p202-p102. The cleavage forms present are markers of caspase-dependent apoptosis. The reduction or loss of caspase proforms can also be a marker of caspase-dependent apoptosis. Caspase activation is followed by cleavage of a myriad of caspase substrates which contributes to the demise and eventual death of the cell. The most highly characterized caspase substrate is PARP. PARP [(ADP-ribose) polymerase] is a 113 kDa nuclear chromatin-associated enzyme that is involved in DNA repair and other cellular events. The cleavage of PARP into an 89 and 28 kDa fragment is considered indicative of functional caspase activation.

Bioinformatics

Alternate Names

Apoptosis Detection apoptosis kinetics apoptosis kit microscopy apoptosis kit