Caspases (cysteine-dependent aspartate specific ptotease) are a family of cysteine proteases that play an essential role in cell apoptosis. Caspases contain a conserved QACXG pentapeptide active site motif and are characterized by specificity for aspartic acid in the P1 position. The synthesis of caspases involves the activation of inactive proenzymes, which contain an N-terminal peptide (prodomain) together with two subunits (one small and one large), following cleavage at specific aspartate cleavage sites. Caspases can be classified into three subfamilies, due to phylogenetic analysis, including an ICE subfamily (caspases-1, -4 and -5), a CED-3/CPP32 subfamily (caspases-3, -6, -7, -8, -9 and -10) and an ICH-1/Nedd2 subfamily (caspase-2).
- A1902 Z-VAD-FMK102 CitationTarget: CaspasesSummary: Cell-permeable, irreversible pan-caspase inhibitor
- A8170 Z-FA-FMKTarget: cysteine proteaseSummary: Cysteine proteases inhibitor
- B3233 Z-LEHD-FMK8 CitationTarget: CaspasesSummary: Irreversible Caspase-9 inhibitor.
- B3232 Z-IETD-FMK12 CitationTarget: CaspasesSummary: Caspase-8 inhibitor
- A9901 Caspase Inhibitor Set ISummary: Caspase Inhibitors
- A8321 Cisplatin5 CitationSummary: Inhibits DNA synthesis,chemotherapy drug
- A8238 VX-7651 CitationTarget: CaspasesSummary: Caspase-1 inhibitor,potent and selective
- A4418 Ac-IEPD-AFCSummary: Recognition motif for serine protease granzyme B
- A4420 PETCMSummary: Caspase-3 activator
- A4417 IvachtinSummary: Caspase-3 inhibitor