Fitc-DQMD-FMK consists of a DQMD motif conjugated to FMK and a FITC dye, enabling fluorescent visualization of enzyme engagement. The construct targets proteases recognizing glutamine- and aspartate-rich motifs. Researchers employ it for kinetic monitoring, active-site mapping, and irreversible inhibition studies. Its fluorescence aids high-sensitivity detection.
CAT No: HB00052
Fitc-DQMD-FMK is a synthetic peptide inhibitor designed for the selective and irreversible inhibition of caspase-3 and related cysteine proteases. As a fluorophore-labeled peptide bearing the FITC (fluorescein isothiocyanate) group, it enables direct visualization and quantification of caspase activity in various experimental systems. The DQMD tetrapeptide sequence is recognized specifically by caspase-3, while the FMK (fluoromethyl ketone) moiety covalently binds to the active site cysteine, effectively blocking enzymatic function. This dual functionality makes Fitc-DQMD-FMK a valuable tool for researchers investigating apoptotic pathways, protease regulation, and cell death mechanisms at both the biochemical and cellular levels.
Apoptosis research: As a potent and selective caspase-3 inhibitor, this labeled peptide is widely employed in apoptosis studies to dissect the role of caspase-3 in programmed cell death. By irreversibly binding to active caspase-3, it allows researchers to temporally control and monitor the inhibition of this key protease, thereby elucidating downstream events in the apoptotic cascade. The FITC label further enables real-time tracking of inhibitor localization and cellular uptake using fluorescence microscopy or flow cytometry, providing spatial and temporal resolution in apoptosis assays.
Protease activity profiling: In biochemical assays, the compound serves as a highly specific probe for profiling caspase-3 and related protease activities in cell lysates or purified enzyme preparations. The fluorogenic tag facilitates direct detection and quantification of enzyme-inhibitor interactions, supporting kinetic studies, inhibitor screening, and the validation of protease substrates. Its irreversible mode of action allows for endpoint measurements that are robust and reproducible, which is particularly advantageous for high-throughput screening formats.
Cell-based assay development: The FITC-conjugated peptide is instrumental in the development of cell-based assays aimed at monitoring caspase activation and inhibition within living cells. Researchers utilize this probe to evaluate the efficacy of novel pro-apoptotic or anti-apoptotic agents, to characterize signaling pathways involving caspase-3, and to assess the impact of genetic modifications on cell death responses. The fluorescence signal provides a convenient and sensitive readout that can be quantified across diverse cell types and experimental conditions.
Mechanistic studies of protease inhibition: Detailed mechanistic investigations benefit from the use of this fluorogenic peptide inhibitor, as it enables the study of caspase-3 substrate recognition, active site accessibility, and inhibitor binding kinetics. By employing the compound in structural or biophysical experiments, scientists can gain insights into the conformational dynamics of protease-inhibitor complexes, map critical residues involved in catalysis, and explore the structural basis for selectivity among caspase family members.
Multiparametric high-content screening: In advanced screening platforms, the FITC-labeled inhibitor is integrated into multiparametric assays that simultaneously assess cell viability, caspase activation, and other apoptotic markers. Its compatibility with automated imaging and flow cytometry technologies allows for large-scale analyses of compound libraries, genetic perturbations, or environmental stressors. The resulting data facilitate the identification of modulators of apoptosis and support drug discovery efforts targeting regulated cell death pathways.
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