Biotin-AEVD-FMK links the AEVD recognition sequence to FMK and a biotin tag. The peptide enables affinity enrichment of proteases recognizing acidic motifs. Researchers use it for substrate mapping, inhibitory profiling, and active-site characterization. Its multifunctional design aids both detection and mechanistic analysis.
CAT No: HB00041
Biotin-AEVD-FMK is a synthetic peptide-based inhibitor that combines a biotinylated N-terminal tag with the tetrapeptide sequence AEVD and a fluoromethyl ketone (FMK) reactive group at the C-terminus. This compound is designed to serve as an irreversible, active-site-directed inhibitor of caspase-10 and related cysteine proteases, exploiting the AEVD motif's selectivity and the FMK group's covalent reactivity. The biotin label enables facile detection, affinity capture, and downstream analysis, making Biotin-AEVD-FMK a valuable probe in apoptosis research, protease activity profiling, and biochemical pathway elucidation. Its tailored structure allows researchers to interrogate caspase-mediated signaling events with high specificity and versatility in a variety of experimental systems.
Enzyme activity profiling: Biotin-AEVD-FMK is widely employed in the detection and quantification of active caspase-10 and related proteases in cell lysates and tissue extracts. By forming a covalent bond with the active site cysteine of target proteases, the inhibitor irreversibly labels enzymatically active molecules. The biotin tag allows for subsequent visualization or enrichment using streptavidin-based methods, supporting sensitive detection in Western blotting, ELISA, or fluorescence-based assays. This approach facilitates detailed profiling of caspase activation dynamics during apoptosis or other cellular processes involving cysteine proteases.
Affinity purification of proteases: The biotin moiety on Biotin-AEVD-FMK enables selective capture of labeled proteases from complex biological samples. After incubation with cell or tissue extracts, the biotinylated inhibitor-protease complexes can be isolated using streptavidin- or avidin-coated matrices. This affinity purification strategy allows for the enrichment and subsequent identification of active protease populations, supporting proteomic studies, substrate identification, and the characterization of enzyme isoforms or post-translational modifications.
Apoptosis pathway investigation: Researchers utilize Biotin-AEVD-FMK to dissect apoptotic signaling cascades by selectively inhibiting and tracking caspase-10 activity. Application of the compound in cell-based assays helps delineate the temporal sequence of caspase activation and the functional consequences of caspase-10 blockade. By enabling both inhibition and detection, the compound provides a dual-function tool for mapping the molecular events underlying programmed cell death, supporting studies in developmental biology, cancer research, and neurobiology.
Inhibitor validation and selectivity studies: The defined peptide sequence and FMK warhead allow Biotin-AEVD-FMK to serve as a benchmark compound in evaluating the specificity and efficacy of novel caspase inhibitors. Researchers can use it in competitive binding assays to compare the potency and selectivity profiles of experimental inhibitors, or to validate assay systems designed to monitor caspase activity. Its well-characterized inhibitory mechanism provides a reference point for interpreting experimental results and optimizing inhibitor design.
Live-cell imaging and localization: The biotinylated inhibitor can be applied in live-cell or fixed-cell imaging experiments to visualize the spatial distribution of active caspase-10 and related proteases. By coupling the biotin tag with fluorescent streptavidin conjugates, researchers can track the subcellular localization and activation patterns of these enzymes during various biological processes. This application supports high-resolution studies of protease dynamics in situ, contributing to a deeper understanding of cellular signaling networks and compartmentalized enzyme activity.
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