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All Dyes is the single product list for the Fluorescent Dyes, Probes & Stains section. Many dyes here have no application or dye-family subcategory, so the list is the broadest way to browse the range. It suits searches by product name when the required dye is already known. Examples range from the near-infrared cyanine indocyanine green and the ratiometric calcium indicator Fura-2 pentapotassium to the nucleic acid stains Hoechst 33258 trihydrochloride and SYBR Green II. Classical stains such as hematoxylin, reactive labeling dyes and enzyme substrates are listed alongside them. For selection by task or by core structure, the parent Fluorescent Dyes, Probes & Stains page groups dyes by application and dye family.
Z-VAN-AMC is a fluorogenic substrate designed for the detection of proteolytic enzymes, particularly those exhibiting legumain-like activity. Upon hydrolysis, Z-VAN-AMC releases a fluorescent signal, making it valuable for studying enzyme activity in various biological systems. Its applications include investigating protease functions in plant-mite interactions and assessing legumains in other biological contexts.
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Cbz-Lys-Lys-PABA-AMC diTFA is a fluorogenic peptide designed to function as a substrate for proteases. It exhibits high specificity for certain enzymes, enabling the detection and quantification of proteolytic activity in biological samples. This compound is valuable in studies requiring the measurement of enzyme kinetics, protease activity, and related metabolic processes.
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Dabsyl-Leu-Gly-Gly-Gly-Ala-Edans is a Dabsyl-labeled peptide designed as a fluorophore substrate for studying peptidase activity. It serves as a specific probe for evaluating the enzymatic activity of the LasA protease from Pseudomonas aeruginosa. This reagent is valuable in research focused on protease function and substrate specificity, facilitating insights into microbial proteolytic mechanisms.
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M-2420 is a fluorogenic substrate designed to target the β-secretase site of the Swedish mutation of amyloid precursor protein (APP). This compound exhibits key biological activity by facilitating the detection and quantification of β-secretase activity, which is crucial for understanding amyloidogenic processes in Alzheimer’s disease. M-2420 is suitable for research applications focused on neurodegenerative diseases and protein cleavage mechanisms.
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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Ac-GAK-AMC is a fluorescent substrate designed to measure protease activity through the hydrolysis of the compound. Upon enzymatic cleavage by proteases, Ac-GAK-AMC releases 7-amino-4-methylcoumarin (AMC), resulting in a detectable fluorescent signal. This reagent is suitable for various research applications, including enzyme assays and studying proteolytic pathways.
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Ala-Phe-Lys-AMC is a fluorogenic substrate designed for the assessment of residual plasmin activity. This compound releases a fluorescent signal upon cleavage, allowing for sensitive detection and quantification of plasmin activity in various biological samples. It is widely utilized in research applications focusing on fibrinolysis and related proteolytic processes.
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4-Methylumbelliferyl β-D-ribofuranoside serves as a fluorogenic substrate for β-ribosidase, a critical enzyme involved in the hydrolysis of ribonucleosides. Its cleavage generates a fluorescent signal, allowing for sensitive detection and quantification of β-ribosidase activity. This compound is widely utilized in biochemical assays and enzyme activity studies, facilitating research in enzymology and cellular metabolism.
MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2 is a fluorescent substrate designed for fluorescence resonance energy transfer (FRET) protease assays. This compound effectively facilitates the measurement of SARS-CoV-2 3CLpro activity, enabling researchers to investigate protease activity in viral infections and assess potential therapeutic interventions. Its use in biochemical assays provides valuable insights into enzyme kinetics and protein interactions in disease models.
Calpain-1 substrate, fluorogenic is a sensitive and specific substrate designed for detecting calpain-1 activity. This substrate is cleaved at the Tyr-Gly bond, resulting in enhanced fluorescence detectable at excitation/emission wavelengths of 490 nm/518 nm. It is valuable in studying calpain-related processes and evaluating the role of calpain-1 in various biological contexts.
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Ac-Gly-Ala-Lys(Ac)-AMC is a fluorogenic substrate designed for the precise measurement of protease activity. Upon hydrolysis, it liberates the fluorescent compound 7-amino-4-methylcoumarin (AMC), which emits a fluorescent signal when exposed to UV light. This reagent is particularly valuable for studies in protease function and activity assays in various biological research applications.
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Suc-YVAD-AMC is a fluorogenic substrate designed for the quantification of cysteine protease activity within the proteasome. Upon cleavage by these enzymes, the compound releases the fluorescent product AMC, enabling sensitive measurement of enzymatic activity. This reagent is widely utilized in research applications focused on proteasomal function and the mechanisms of protein degradation.
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Boc-Leu-Ser-Thr-Arg-AMC is a fluorogenic substrate designed for the detection of protease activity. Its amino acid sequence is optimized for specificity, enabling enhanced fluorescence upon cleavage by various proteases. This compound serves as a valuable tool for studying proteolytic processes in biochemical research and assays.
