Human/Mouse Caspase-7 Antibody

Caspase-7 (Cysteine-aspartic acid protease 7/Casp7; also CMH-1, ICE-LAP3 and Mch3) is a 32 kDa member of the peptidase C14A/IL-1 beta-converting family of enzymes (1, 2, 3). It is widely expressed, except in brain, and is best known as an integral component of the apoptotic cascade. Caspase-7 is considered to be an executioner caspase, as a downstream mediator of apoptotic-associated proteolysis (2, 3). Upon activation, Caspase-7 is known to utilize a Cys residue to cleave multiple substrates, including PARP, procaspase 6, Gas2 and calpstatin (1). Human procaspase-7 is a 34 - 36 kDa, 303 amino acid (aa) protein (4, 5, 6). Normally, it is an inactive homodimer (1, 2, 7, 8). But following an upstream signal that activates processing proteases, procaspase-7 undergoes proteolytic cleavage to generate an N-terminal 23 aa propeptide, a 175 aa p20/20 kDa subunit (aa 24 - 198), and a 105 aa C-terminal p12/12 kDa subunit (5). The p20 and p12 subunits noncovalently heterodimerize, and subsequently associate with another p20/p12 heterodimer to form an active antiparallel homodimer. Additional processing of p20 may remove aa 24 - 36 to generate p18, while additional processing of p12 will remove aa 199 - 206 to generate p11 (9, 10). Multiple proteases can use Caspase-7 as a substrate, and include caspase-1, -3, -8, and -10, granzyme B, calpain-1 and Caspase-7 itself (3, 6, 9, 11). Caspase-7 is found in both cytosol and nucleus, and possesses a potential KKKK nuclear localization signal between aa 38 - 41 that likely undergoes sumoylation (9, 12). There are two potential isoform variants, one which shows an alternate start site 33 aa upstream of the standard start site, and a second that shows a 105 aa substitution for aa 149 - 303. Human and mouse Caspase-7 are 82% aa identical at the amino acid level.