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    Caspase / Apoptosis Inhibitors

    CAS-BIND™ Pro inhibitors (*) have been optimized for greater performance, potency and cell permeability.

    Caspase Inhibitors of Apoptosis Recognition Sequence
    CAS-BIND™ P  Pan Caspase Inhibitor z-VAD-FMK
    *CAS-BIND™ Pro Premium, more potent Pan Caspase Inhibitor Pro-VAD-FMK
    CAS-BIND™  Caspase-1 Inhibitor z-WEHD-FMK
    CAS-BIND™  Caspase-3 Inhibitor z-DEVD-FMK
    CAS-BIND™  Caspase-9 Inhibitor  z-LEHD-FMK

    Members of the caspase enzyme family (cysteine proteases with aspartate specificity) play significant roles in both inflammation and apoptosis. Caspases exhibit catalytic and substrate-recognition motifs that have been highly conserved. These characteristic amino acid sequences allow caspases to interact with both positive and negative regulators of their activity. The substrate preferences or specificities of individual caspases have been exploited for the development of peptides that successfully compete for caspase binding while maintaining their distinctive aspartate cleavage sites at the P1 position.

    It is possible to generate inhibitors of caspase activation by coupling caspase-specific peptides to certain aldehyde, nitrile or ketone compounds. Fluoro-methyl ketone (FMK)-derivatized peptides act as effective irreversible inhibitors with no added cytotoxic effects. Inhibitors synthesized with a benzyloxy-carbonyl group (also known as a “Z” group) at the N-terminus and methyl esters exhibit enhanced cellular permeability. These peptide inhibitors are cell-permeant and bind irreversibly to active caspases inside the cell, effectively inhibiting cell death (e.g. apoptosis, pyroptosis) and inflammatory pathways.