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    Pan Caspase (z-VAD) Inhibitor

    Sequence: Z-VAD-FMK
    Size: 1 mg
    Storage: -20° C

    The CAS-BIND™ Pan Caspase (Z-VAD-FMK) inhibitor is a cell-permeable inhibitor that forms an irreversible covalent bond with active caspases inside the cell. The activation of caspases is a hallmark event in apoptosis. To inhibit apoptosis in cell culture assays, the inhibitor should be added prior to induction of apoptosis. 

    Target: Pan Caspase
    Sequence/Synonyms: Z-VAD(Ome)-FMK, Z-Val-Ala-Asp(OMe)-FMK
    Formula: C22H30FN3O7
    Chemical Name: Carbobenzyloxy-L-valyl-L-alanyl-L-aspartic acid methyl ester fluoromethyl ketone
    Molecular Weight: 467.49 amu
    Working Concentration: 1 uM - 100 uM, optimize for each assay/model

    Kit Components:
    Z-VAD-FMK, 1 vial

    MSDS (PDF)


    The product should be reconstituted using high grade anhydrous DMSO. The product may not be visible in the vial prior to reconstitution. When lyophilized the product may create a thin film on the inside of the vial. Ensure that the reagent is fully in solution before using.

    General Information:

    • The inhibitors should be added prior to inducing caspase activity.
    • High concentrations of DMSO can be toxic to cells, therefore, DMSO should be diluted so that the final concentration in the cell culture is less than 1%, or a suitable control made.
    • The product should be diluted using PBS with 1% BSA or a suitable alternative, based on experience.
    • Final working concentrations between 1 µM and 100 µM have been successfully used to inhibit caspase activity.

     All experiments involve many variables. The researcher should use their experience to determine the best and most effective concentration for their specific research application.

    Background Information:

    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 reversible or irreversible inhibitors of caspase activation by coupling caspase-specific peptides to certain aldehyde, nitrile or ketone compounds. Fluoromethyl ketone (FMK)-derivatized peptides act as effective irreversible inhibitors with no added cytotoxic effects. Inhibitors synthesized with a benzyloxycarbonyl group (also known as a “Z” group) at the N-terminus and methyl esters exhibit enhanced cellular permeability.