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Browse coumarin dyes and derivatives identified in product-specific catalog or supplier information. Compare individual product specifications and package options.
The family grouping does not establish a shared excitation wavelength, enzyme specificity or labeling function. Review the documented use of the exact derivative.
Synonyms: 7-Ethoxycoumarin-3-carbonitrile
3-Cyano-7-ethoxycoumarin is a fluorogenic substrate suitable for the continuous determination of cytochrome P450 mixed-function monooxygenases. It is a fluorescent probe useful in microsomal dealkylase studies.
Z-Gly-Gly-Arg-AMC is a thrombin-specific chromogenic substrate that enables the study of thrombin generation in platelet-rich plasma (PRP) and platelet-poor plasma (PPP). This fluorogenic substrate has an excitation/emission maximum at 390/480 nm, facilitating sensitive detection of thrombin activity. It is widely utilized in research applications focused on coagulation and thrombotic disorders.
7-Ethoxy-4-methylcoumarin acts as a substrate probe for mammalian cytochrome P450 enzymes, specifically targeting CYP1A1, CYP2B4, and CYP2B6. This coumarin derivative is widely used in research to study enzymatic activity and metabolic pathways involving these cytochrome P450 isoforms. Its ability to provide insights into drug metabolism and toxicity makes it a valuable tool in pharmacological and toxicological studies.
6,7-Diethoxy-4-methylcoumarin is a fluorogenic substrate utilized for studying enzymatic activity. This compound exhibits fluorescent properties upon enzymatic conversion, making it useful in the detection and quantification of various enzymes in biological samples. Its application extends to areas such as drug metabolism studies and biological research involving Cordyceps militaris metabolites.
Succinimide-AFK-AMC acetate is a fluorescent substrate that targets Pseudomonas aeruginosa protease activity. This compound is utilized as a biomarker for identifying and quantifying protease production in cultured reference strains. It is particularly valuable for research on bacterial virulence and pathogenesis, enabling detailed study of protease-related mechanisms in infection models.
Z-Gly-Gly-Leu-AMC is a selective substrate for ClpP1 and ClpP2 proteolytic activity. This compound is utilized to monitor and quantify the enzymatic activity of ClpP in conjunction with the activating peptide Z-Leu-Leu. Its application is crucial for research focused on protease activity, protein degradation pathways, and associated cellular processes.
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L-Pyroglutamic acid 7-amido-4-methylcoumarin serves as a fluorogenic substrate for pyroglutamate aminopeptidase 1 (PGP-1). This compound exhibits biological activity by enabling the detection of PGP-1 enzymatic activity through fluorescence development. It is primarily utilized in biochemical assays for characterizing the enzyme's function and studying related pathways in research applications.
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Synonyms: 7-BFC
7-Benzyloxy-4-(trifluoromethyl)coumarin (7-BFC) is a coumarin-based fluorescent substrate utilized for the evaluation of cytochrome P450 enzymes CYP1A2 and CYP3A4. Upon metabolism, 7-BFC is converted into 7-hydroxy-4-trifluoromethylcoumarin (HFC). This compound is valuable for conducting rapid screening of CYP isoform metabolism and inhibition assays in pharmacological research.
Synonyms: 7-HCA; Umbelliferyl Arachidonate; 7-HC-arachidonate
7-Hydroxycoumarinyl arachidonate is a fluorogenic substrate for cytosolic phospholipase A2 (PLA2) and monoacylglycerol lipase (MAGL). Upon hydrolysis, it generates arachidonic acid (AA) and the highly fluorescent product 7-hydroxyl coumarin (7-HC). The production of 7-HC can be quantitatively assessed using a fluorometer, making this compound valuable for studies investigating the enzymatic activity of PLA2 and MAGL in various biological contexts.
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Pyr-Arg-Thr-Lys-Arg-AMC is a chromogenic substrate for proteolytic enzymes, primarily hydrolyzed by trypsin and thrombin. This peptide serves as a valuable tool for quantifying the activity of these proteases, as well as assessing the efficacy of enzyme inhibitors. Its use in biochemical assays enables researchers to explore protease function and regulation in various biological contexts.
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H-Gly-Gly-Arg-AMC is a fluorogenic substrate designed for the continuous assessment of thrombin generation. This compound features a C-terminal 7-amino-4-methylcoumarin (AMC) moiety, which fluoresces upon cleavage. It is employed in research applications focusing on coagulation pathways and thrombin activity, enabling precise monitoring of thrombin dynamics in biological samples.
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Suc-GPLGP-AMC is a specific peptide substrate for collagenase-like peptidases. It serves as a valuable tool for studying the enzymatic activity of these peptidases in biological research. This compound is frequently utilized in assays to monitor and quantify collagenase activity, facilitating the investigation of processes such as tissue remodeling and wound healing.
4-Methylumbelliferyl butyrate is a coumarin-based fluorogenic substrate primarily utilized for the identification of Moraxella catarrhalis C4-esterase. Upon enzymatic cleavage, it is converted to the highly fluorescent 4-methylumbelliferone, enabling sensitive detection and quantification of enzymatic activity. This reagent is valuable in biochemical assays and research applications involving enzyme kinetics and substrate specificity.
Ac-IEPD-AMC is a fluorogenic substrate designed for the quantification of protease activity. Upon hydrolysis, Ac-IEPD-AMC releases the fluorescent molecule 7-amino-4-methylcoumarin (AMC), which exhibits strong fluorescence under UV illumination. This compound is valuable for investigating proteolytic enzyme functions and can be utilized in various assays to measure protease activities in biological samples.
Z-VDVAD-AFC is a fluorogenic substrate designed to measure the activity of cysteine protease 3 (Caspase-3). Upon hydrolysis, Z-VDVAD-AFC releases 7-amino-4-trifluoromethylcoumarin (AFC), which exhibits strong fluorescence under ultraviolet light. This property enables researchers to monitor proteolytic activity in various biological assays, facilitating studies in apoptosis, cell signaling, and disease mechanisms.
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