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Enzyme Activity Probes & Substrates
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.
Gly-Phe-AMC is a fluorogenic peptide substrate that consists of a glycine-phenylalanine sequence linked to the fluorophore AMC. This compound is specifically utilized as a substrate for cathepsin C and is instrumental in detecting the activity of various proteases. Its ability to fluoresce upon cleavage makes Gly-Phe-AMC a valuable tool in biochemical assays and protease activity studies.
TOPS is a chromogenic substrate that participates in an oxidative coupling reaction with 4-aminoantipyrine in the presence of hydrogen peroxide and nanocrystalline cobalt selenide. This compound serves as an essential tool for the detection of uric acid, enabling studies related to purine metabolism and related disorders. Its specific reactivity and capacity to produce measurable color changes make TOPS valuable for various biochemical analyses and diagnostics.
D-Ile-Pro-Arg p-nitroanilide dihydrochloride serves as a chromogenic peptide substrate for tissue plasminogen activator (tPA). This compound enables the study of tPA activity through the quantification of its enzymatic cleavage, facilitating investigations into fibrinolytic processes. It is commonly utilized in research applications focused on thrombolysis and related cardiovascular studies.
Me-CO-Lys(Cbo)-Gly-Arg-pNA is a specific substrate for C1 esterase, facilitating the study of this enzyme's catalytic action. It is designed to yield a cleavage product that can be quantitatively measured, enabling researchers to investigate C1 esterase activity in various biological contexts. This compound is valuable for assays aimed at understanding enzymatic processes and exploring potential therapeutic applications related to C1 esterase dysfunction.
Bz-Ala-Arg is a dipeptide that acts as a substrate for human pancreatic carboxypeptidase B and plasma carboxypeptidase N. It is utilized in biochemical research to study proteolytic enzyme activity and the regulation of protein metabolism. This compound is valuable for investigating the enzymatic characteristics and kinetics of carboxypeptidases in various physiological and pathological contexts.
Resorufin-β-D-glucopyranoside is a fluorogenic substrate specifically designed for the detection and quantification of β-glucosidase activity. Upon enzymatic cleavage, it produces resorufin, a highly fluorescent compound that serves as an effective indicator of β-glucosidase presence in biological samples. This reagent is widely used in biochemical assays and studies involving enzyme activity, providing valuable insights into cellular and molecular processes.
Ac-LEVD-AFC is a fluorogenic substrate peptide specifically designed for the activity assays of caspase-4. This compound exhibits key biological activity by releasing a fluorescent signal upon cleavage by caspase-4, making it a valuable tool for studying apoptosis and inflammatory processes. It is suitable for various research applications, including cell death studies and the evaluation of caspase activity in different biological systems.
4-Methylumbelliferyl 2-acetamido-2-deoxy-α-D-galactopyranoside serves as a fluorogenic substrate for the assessment of α-galactosidase enzymatic activity. This compound is integral for analyzing enzyme kinetics in various biological samples, providing insights into the physiological roles of α-galactosidase. Additionally, it can be utilized for screening potential inhibitors or activators of this enzyme, facilitating research into its regulatory mechanisms and therapeutic targets.
4-Methylumbelliferyl stearate is a biochemical reagent commonly utilized as a fluorogenic substrate for the detection of lipase activity. Upon enzymatic hydrolysis, it releases the fluorescent compound 4-methylumbelliferone, facilitating quantitative analysis of lipase in various biological samples. This reagent is widely employed in research applications focusing on lipid metabolism, enzyme kinetics, and the study of lipid-related disorders.
NOBA is a synthetic chromogenic substrate designed for the detection of AplTX-II enzyme activity. It facilitates the study of phospholipid hydrolysis and is valuable for research applications focused on enzymatic processes involving phospholipids. Researchers can utilize NOBA to gain insights into the functional dynamics of AplTX-II in various biological contexts.
4-Trifluoromethylumbelliferyl-ß-D-galactopyranoside (TFMU-Gal) is a fluorogenic substrate primarily used in biochemical assays for the detection of ß-galactosidase activity. Upon enzymatic cleavage, TFMU-Gal releases a highly fluorescent product, making it a valuable tool in glycobiology research for studying glycosidase activity and carbohydrate metabolism. This compound is essential for understanding the role of glycosides in various biological processes.
Boc-Val-Gly-Arg-AMC is a peptide substrate designed for the analysis of proteasome activity. This compound serves as a sensitive fluorogenic reporter, enabling the quantification of proteolytic processes in biological samples. Its utility extends to various research applications, including drug discovery and the study of cellular protein degradation mechanisms.
4-Methylumbelliferyl β-D-fucoside is a fluorogenic substrate for the enzymatic detection of fucosidase activity. Upon hydrolysis by fucosidases, it releases 4-methylumbelliferone, which exhibits high fluorescent properties. This reagent is widely used in biochemical assays to study fucosidase activity in various biological samples, facilitating research in glycoprotein metabolism and cellular signaling pathways.
4-Methylumbelliferyl β-L-fucoside is a fucose derivative functioning as a fluorogenic substrate for β-L-fucosidase activity. This compound releases a fluorescent product upon cleavage, making it suitable for biochemical assays and glycobiology research. It enables the study of glycan metabolism and the characterization of fucosylated biomolecules, facilitating research in various biological systems.
4-Methylumbelliferyl 3,4,6-tri-O-acetyl-2-deoxy-2-trifluoroacetamido-α-D-glucopyranoside functions as a fluorogenic substrate for carbohydrate-active enzymes, specifically glycosidases. This compound enables the quantitative detection of glycosidase activity through fluorescence emission, making it valuable in enzymology and carbohydrate metabolism research. It aids in studying enzymatic reactions and the characterization of glycosidase specificity, contributing to a better understanding of glycosylation processes in biological systems.
4-Methylumbelliferyl-β-D-lactoside is a fluorogenic substrate primarily targeting β-galactosidase, facilitating the study of enzyme activity in glycobiology. This compound is widely utilized in biochemical assays for the detection and quantification of β-galactosidase activity, making it valuable for research applications involving carbohydrate metabolism and glycan interactions.
Z-Gly-Pro-Gly-Gly-Pro-Ala-OH serves as a collagenase substrate, enabling the study of collagenase activity and its effects on cellular processes. This compound is utilized in research focusing on biomaterial interactions and tissue engineering, particularly in the context of planulae settlement. Its unique peptide structure facilitates targeted enzymatic cleavage, making it a valuable tool for investigating collagen dynamics in various biological systems.
pGlu-Pro-Arg-MNA is a chromogenic substrate designed for use in enzyme assays. It serves as a substrate for various proteolytic enzymes, facilitating the study of enzyme kinetics and activity. This compound is particularly valuable in research applications involving protease activity, enabling researchers to investigate proteolytic processes in biochemical studies.
D-Val-Leu-Lys-pNA is a chromogenic peptide substrate targeting plasmin and plasminogen. This compound serves as a sensitive substrate for the DFE27 serine protease from Bacillus subtilis DC27. Upon catalysis by plasmin, D-Val-Leu-Lys-pNA undergoes hydrolysis, releasing p-nitroaniline (pNA), which can be quantitatively detected at 405 nm, making it a valuable tool for assessing fibrinolytic activity in biochemical research.
7-Methyl-6-thioguanosine (MESG) serves as a chromogenic substrate for purine nucleoside phosphorylase, converting to 7-methyl-6-thioguanine in the presence of inorganic phosphate. This compound is instrumental in quantifying inorganic phosphate levels, making it valuable for studies involving nucleotide metabolism. Additionally, MESG can be utilized to assess the activity of purine nucleoside phosphorylase and protein phosphatases in various biochemical assays, facilitating research in enzymology and cellular signaling pathways.
Fluorescent Substrate for Glu-Specific Proteases is designed as a chromogenic substrate specifically for V8 protease. It exhibits fluorescence upon cleavage, allowing for easy monitoring of protease activity. This substrate is useful in biochemical assays aimed at studying enzymatic mechanisms and the role of V8 protease in various biological processes.
Abz-Thr-Ile-Nle-p-nitro-Phe-Gln-Arg-NH2 is a fluorogenic substrate designed for use in fluorescence-based screening assays. This compound exhibits enhanced fluorescence upon enzymatic cleavage, making it suitable for the study of enzymatic activity and proteolytic processes. Its applications extend to substrate specificity assays and the characterization of proteases in various biological research contexts.
Lys-Pro-AMC is a fluorogenic substrate designed for the detection and quantification of specific enzyme activities. Upon cleavage by target enzymes, it releases a highly fluorescent product that can be easily measured, providing a sensitive assay for enzyme kinetics and activity. This substrate is useful in various research applications, including enzyme characterization, drug screening, and biochemical studies focused on proteolytic activity.
Bz-RGFFL-4MβNA is a fluorogenic peptide substrate with the sequence Bz-Arg-Gly-Phe-Phe-Leu-4MβNA. This compound is designed for use in enzymatic assays and can facilitate the study of protease activity. Its unique fluorescent properties allow for sensitive detection and quantification in various biological research applications, providing valuable insights into cellular processes and enzyme kinetics.
Abz-GFDPFRQ-EDDnp is a fluorogenic substrate targeting metallothionein oligopeptidase, with excitation and emission wavelengths of 320 nm and 420 nm, respectively. This compound is instrumental in assessing the enzymatic activity of metallothionein oligopeptidase in tissue extracts. Its applications extend to research studies focused on temporal lobe epilepsy, facilitating insights into the enzyme's role in neurological processes.
