FITC-ATAD-FMK is cell permeable, non-toxic, and irreversibly binds to activated caspase-12 in apoptotic cells.
CAT No: HB00028
Fitc-ATAD-FMK is a synthetic peptide inhibitor featuring a fluorescein isothiocyanate (FITC) label and a fluoromethyl ketone (FMK) reactive group, designed for targeted and irreversible binding to specific cysteine proteases. As a cell-permeable, activity-based probe, it is widely utilized in apoptosis research and protease activity profiling due to its ability to covalently modify active sites of caspases and related enzymes. The FITC moiety confers intrinsic fluorescence, enabling direct visualization and quantification in a range of biochemical and cell-based assays. Its structural design integrates both selectivity and traceability, making it a valuable tool for dissecting proteolytic mechanisms and monitoring enzyme dynamics in complex biological systems.
Protease Activity Profiling: In the context of enzyme research, Fitc-ATAD-FMK serves as a highly effective probe for labeling and detecting active cysteine proteases, particularly caspases implicated in programmed cell death pathways. By covalently binding to the catalytic site of active enzymes, it allows researchers to monitor protease activation states in real time. The fluorescent tag facilitates direct detection using fluorescence microscopy, flow cytometry, or plate-based assays, supporting detailed examination of protease regulation under physiological or experimental conditions.
Apoptosis Detection: The compound is extensively applied in apoptosis studies, where its ability to selectively label active caspases provides a sensitive means to identify and quantify apoptotic cells. Upon entering cells, the FMK moiety reacts with the active site of executioner caspases, and the FITC label enables subsequent detection. This approach offers a robust alternative to traditional antibody-based methods, delivering high specificity and compatibility with multiplexed analysis for elucidating apoptosis kinetics and pathway modulation.
Cell-Based Assay Development: Fitc-ATAD-FMK is instrumental in the development and optimization of cell-based assays for high-throughput screening or mechanistic studies. Its cell-permeable nature ensures efficient intracellular delivery, while the fluorescent signal supports quantitative analysis of enzyme inhibition, pathway activation, or compound efficacy. This utility is particularly valuable in drug discovery and target validation workflows, where accurate measurement of protease activity is critical for evaluating potential modulators or identifying off-target effects.
Mechanistic Enzyme Studies: The compound's irreversible binding mechanism enables detailed mechanistic investigations of cysteine protease function, substrate specificity, and inhibitor selectivity. By providing a stable, covalently modified enzyme population, it supports kinetic studies, structural analysis, and the mapping of active site residues. Researchers leverage these capabilities to gain insights into protease regulation, allosteric modulation, and the molecular basis of enzyme-inhibitor interactions.
Fluorescence-Based Imaging and Quantification: The integrated FITC label allows for direct visualization and quantification of labeled proteases in live or fixed cells, tissue sections, or cell extracts. This fluorescence-based approach not only streamlines experimental workflows but also enhances spatial and temporal resolution in imaging studies. Applications include tracking protease dynamics during cellular stress responses, mapping subcellular localization of proteolytic activity, and correlating enzyme activation with phenotypic changes in diverse biological models.
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