Caspase
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).
- A4416 AZ 10417808Target: CaspasesSummary: Caspase-3 inhibitor,selective non-peptide
- A4417 IvachtinSummary: Caspase-3 inhibitor
- A4420 PETCMSummary: Caspase-3 activator
- A4418 Ac-IEPD-AFCSummary: Recognition motif for serine protease granzyme B
- A8238 VX-7651 CitationTarget: CaspasesSummary: Caspase-1 inhibitor,potent and selective
- A8321 Cisplatin5 CitationSummary: Inhibits DNA synthesis,chemotherapy drug
- A9901 Caspase Inhibitor Set ISummary: Caspase Inhibitors
- B3232 Z-IETD-FMK12 CitationTarget: CaspasesSummary: Caspase-8 inhibitor
- B3233 Z-LEHD-FMK8 CitationTarget: CaspasesSummary: Irreversible Caspase-9 inhibitor.
- A1902 Z-VAD-FMK102 CitationTarget: CaspasesSummary: Cell-permeable, irreversible pan-caspase inhibitor