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Browse substrates and optical reporter reagents for enzyme-activity assays. Enzyme-activated fluorogenic probes can convert a chemical transformation into a fluorescence readout.[1] Choose the exact reagent for your enzyme, sample and detection method, and distinguish fluorescent from color-based readouts. This collection does not imply that every substrate is selective for one enzyme or suitable for use in living cells.
[1] Chyan W, Raines RT. Enzyme-Activated Fluorogenic Probes for Live-Cell and in Vivo Imaging. ACS Chemical Biology. 2018;13(7):1810–1823. DOI: 10.1021/acschembio.8b00371. PMID: 29924581; PMCID: PMC6056172.
Ac-VQVD-pNA is a chromogenic substrate specifically designed for the detection of caspase 3 activity. When cleaved by caspase 3, it releases p-nitroaniline, which can be quantitatively measured. This reagent is valuable for studying apoptosis and cell death pathways in various biological research applications.
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Dabcyl-GLRTQSFS-EDANS is a fluorogenic peptide substrate designed to assess the enzymatic activity of Hepatitis A Virus 3C proteinase. This substrate provides a means to study proteolytic processes and the dynamics of viral infections. Its fluorescent characteristics enable the sensitive detection of enzymatic cleavage, making it a valuable tool in virology research and drug development studies.
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Ac-RSLK-AMC is a fluorogenic peptide substrate designed to target site-1 protease (S1P). It serves as a powerful tool for quantifying the enzymatic activity of S1P in biochemical assays. This reagent is instrumental in studies related to proteolytic processing, providing insights into cellular mechanisms and regulatory pathways influenced by S1P activity.
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Gly-Arg-pNA is a fluorogenic substrate utilized for the assessment of protease activity. Upon hydrolysis, it releases p-nitroaniline, a compound that exhibits fluorescence under ultraviolet light. This property enables the quantification of protease activity through the measurement of emitted fluorescent signals, making it a valuable tool in biochemical and molecular research applications.
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Mca-PLA-Nva-Dap(Dnp)-AR-NH2 is a fluorogenic substrate specifically designed for the matrix metalloproteinase-2 (MMP-2). It enables real-time monitoring of MMP-2 activity through fluorescence, making it useful for studying proteolytic processes in various biological contexts. This substrate is valuable in research applications focusing on cancer metastasis, wound healing, and extracellular matrix remodeling.
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Bacterial Sortase Substrate III, Abz/DNP is a fluorescent peptide substrate designed for the study of Sortase A activity. This substrate undergoes cleavage by Staphylococcus aureus Sortase A (SrtAΔN24) and Streptococcus pyogenes Sortase A (SrtAΔN81), facilitating the formation of an amide bond between the carboxyl group of threonine and the amino group of the cell wall cross-bridge. The cleavage event can be monitored by fluorescence with excitation and emission wavelengths at 320 nm and 420 nm, respectively, making it a valuable tool in investigating sortase-mediated processes.
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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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Mca-KPLGL-Dap(Dnp)-AR-NH2 TFA is a fluorogenic substrate specifically designed for matrix metalloproteinases (MMPs). Upon cleavage by MMPs, 7-methoxycoumarin-4 acetyl (Mac) is released, exhibiting fluorescence that can be quantified to assess MMP activity. This substrate is particularly useful in studying the role of MMPs in various biological processes and diseases. Mac shows excitation and emission wavelengths at 328 nm and 420 nm, respectively, facilitating sensitive detection in biochemical assays.
Boc-Glu(OBzl)-Gly-Arg-AMC is a fluorogenic substrate specifically designed for the detection of factors IXa and XIIa. Upon enzymatic cleavage of the amide bond between arginine and the methylcoumarin amide moiety, it releases the fluorescent compound 7-Amino-4-methylcoumarin. This substrate is valuable for biochemical assays focused on studying coagulation pathways and enzyme activity.
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TRH-AMC serves as a fluorogenic substrate specifically for the enzyme that degrades thyrotropin-releasing hormone (TRH). By utilizing this substrate in coupled assays, researchers can effectively study the biochemical activity of TRH-degrading ectoenzymes. This compound is valuable for investigating the enzymatic processes involved in hormonal regulation and related physiological pathways.
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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.
DNP-Pro-Leu-Ala-Leu-Trp-Ala-Arg-OH is a synthetic peptide substrate targeting matrix metalloproteinase MMP-1, exhibiting a Km of 26.61 μM. This compound serves as a fluorescence probe to detect and monitor protein activity, making it valuable for research applications in enzyme kinetics and protease activity studies. Its effective use in fluorescence assays facilitates the exploration of biological processes involving metalloproteinases.
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Ala-Ala-Phe-AMC TFA is a fluorogenic substrate utilized for the assessment of tri-peptidyl peptidase II (TPPII) activity. This compound provides a sensitive tool for monitoring enzymatic activity, facilitating research in proteolytic processes and related biological pathways. Its fluorescent properties make it valuable for various applications in biochemical assays and enzyme kinetics studies.
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.
Dansyl-D-Ala-Gly-Phe(pNO2)-Gly is a synthetic peptide substrate designed for use as a fluorescent dye. It selectively targets neutral endopeptidase (NEP), which recognizes and cleaves the peptide, releasing the fluorescent dansyl group. This property enables quantitative assessment of NEP activity, making it a valuable tool in research focused on enzyme kinetics and functional assays involving NEP modulation.
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Synonyms: S-2238 dihydrochloride
H-D-Phe-Pip-Arg-pNA dihydrochloride is a chromogenic substrate specifically designed for thrombin activity assessment. It is based on the N-terminal sequence of the A alpha chain of fibrinogen, the natural substrate for thrombin. This reagent facilitates the measurement of antithrombin-heparin cofactor (AT-III) levels, providing a sensitive, accurate, and straightforward method for applications in coagulation research and diagnostics.
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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Protein kinase affinity probe 1 is a specialized affinity probe designed for the functional identification and characterization of protein kinases (PKs). This compound is a modified form of Purvalanol B, featuring a 50% bead loading which enhances its efficacy in isolating target proteins. Its primary applications include studying kinase activity, investigating signaling pathways, and facilitating the development of kinase inhibitors in various biological research settings.
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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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Synonyms: Dabcyl-CMV-Edans
Dabcyl-RGVVNASSRLA-Edans is a fluorogenic substrate specifically designed for the detection of human cytomegalovirus (HCMV) protease activity. This compound exhibits a significant fluorescent response upon cleavage, facilitating real-time monitoring of protease activity in biological samples. Its utility extends to research applications involving HCMV pathogenesis and the development of antiviral therapies.
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Synonyms: Gly-Arg-4-NA hydrochloride; GR-pNA hydrochloride; GR p-itoailide hydrochloride
H-Gly-Arg-pNA hydrochloride is a fluorescent dye that serves as a colorimetric substrate for thrombin. This compound is specifically cleaved by thrombin, releasing p-nitroaniline (pNA), which can be detected colorimetrically at 405 nm. H-Gly-Arg-pNA hydrochloride is widely utilized in assays for measuring thrombin activity, providing valuable insights into coagulation processes and related research applications.
