Caspase-7, a member of the caspase (cysteine aspartate protease) family of proteins, has been shown to be an executioner protein of apoptosis upon cell death stimuli. During apoptosis, caspase-7 is activated through proteolytic processing at conserved aspartic residues by upstream enzymes, including caspase-3, -6, -8, and -9 and granzyme B. Active caspase 7 is in the form of a heterotetramer with 2 large and 2 small subunits. As an effector caspase similar to caspase-3, caspase-7 cleaves downstream substrates like poly (ADP-ribose) polymerase (PARP) through the recognition sequence DEVD.
Anti-Human cleaved Caspase 7 (D6H1)-152Sm—50 Tests