Fitc-AEVD-FMK presents an AEVD sequence linked to FMK and a FITC fluorophore. The peptide targets proteases with selectivity for acidic and hydrophobic motifs. Researchers employ it for fluorescent labeling of active enzymes and kinetic monitoring. Its modular design supports mechanistic and imaging studies.
CAT No: HB00040
Fitc-AEVD-FMK is a synthetic peptide inhibitor that incorporates a fluoromethyl ketone (FMK) reactive group and is covalently labeled with fluorescein isothiocyanate (FITC) at the N-terminus. Structurally, it is designed to specifically target and irreversibly inhibit caspase-10, an initiator caspase involved in the extrinsic apoptotic pathway. The AEVD tetrapeptide sequence confers selectivity, while the FITC label allows for direct visualization and quantification in fluorescence-based assays. This dual-functionality makes the compound a valuable molecular tool for dissecting caspase-mediated signaling events, mapping apoptotic pathways, and facilitating high-resolution biochemical analyses in cell and molecular biology research.
Apoptosis research: As a cell-permeable, irreversible caspase-10 inhibitor, Fitc-AEVD-FMK is widely utilized in studies investigating programmed cell death mechanisms. By selectively blocking caspase-10 activity, researchers can delineate its specific role in the initiation and propagation of apoptosis, particularly in response to death receptor signaling. The inhibitor enables the functional dissection of caspase cascades, helping to distinguish upstream and downstream events and to clarify cross-talk between extrinsic and intrinsic apoptotic pathways. Its use is especially relevant in cellular models where precise temporal and spatial control of caspase activity is required to unravel complex cell death networks.
Fluorescence-based detection: The FITC moiety on Fitc-AEVD-FMK allows for the direct visualization of caspase-10 activity within live cells or tissue samples. Upon binding and covalent modification of active caspase-10, the fluorescent signal can be monitored using flow cytometry, confocal microscopy, or fluorescence plate readers. This enables real-time tracking of enzyme activity, subcellular localization, and dynamic changes in response to experimental stimuli. The high sensitivity and specificity of fluorescence detection facilitate quantitative analysis and single-cell resolution, making the compound a preferred choice for advanced cell biology experiments.
Enzyme activity profiling: The irreversible binding mechanism of the FMK group in Fitc-AEVD-FMK provides a robust approach for profiling active caspase-10 populations in complex biological samples. By selectively labeling only the active form of the enzyme, the inhibitor supports studies focused on enzyme activation kinetics, substrate specificity, and the identification of regulatory factors. This application is particularly valuable in the context of drug discovery, where screening for modulators of caspase-10 activity requires sensitive and selective detection methods.
Pathway mapping and signal transduction studies: In experimental systems where multiple caspases are activated in parallel, Fitc-AEVD-FMK serves as a powerful tool for dissecting signaling hierarchies. By selectively inhibiting caspase-10, researchers can determine its contribution to downstream effector activation, mitochondrial events, and the interplay with other protease families. This enables the construction of detailed molecular maps of apoptotic and non-apoptotic signaling pathways, supporting the development of targeted intervention strategies in basic and applied research.
Validation of biochemical assays: The dual functionality of Fitc-AEVD-FMK as both an inhibitor and a fluorescent probe supports its use in assay development and validation. It is routinely employed as a positive control in caspase-10 activity assays, ensuring assay specificity and sensitivity. Additionally, the compound aids in troubleshooting and optimizing experimental conditions by providing a reliable means to confirm enzyme inhibition and signal detection in a variety of biochemical and cell-based platforms.
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