enzymatic

Malachite green oxalate is a triphenylmethane dye which can be used to detect the release of phosphate in enzymatic reactions.

DHBS (DCHBS) is used in conjunction with 4-aminoantipyrine (4-AAP) and H2O2 for chromogenic quantitation of peroxidase in coupled enzymatic reactions.

PNPG (4-Nitrophenyl β-D-glucopyranoside) is a chromogenic substrate for β-D-glucosidase that, upon enzymatic cleavage, yields a yellow solution.

TMB-PS (TMBZ-PS) is a chromogenic reagent for the detection of hydrogen peroxide e.g. in the enzymatic analysis of body fluids.

5(6)-CFDA (5-(6)-Carboxyfluorescein diacetate) is a cell-permeant esterase substrate that can serve as a viability probe that measures both enzymatic activities, which is required to activate its fluorescence, and cell-membrane integrity, which is required for intracellular retention of their fluorescent product.

WST-1 is a cytotoxic, water-soluble tetrazolium salt that induces intracellular mitochondrial dehydrogenases to undergo NADH-dependent enzymatic reactions, releasing water-soluble methylbenzene products.WST-1 can be used to detect cell proliferation and cellular activity by assaying the uptake values, and can be used to determine superoxide dismutase activity in the WST-1 plate assay.

FAM amine, 5-isomer is a fluorescein linker capable of undergoing enzymatic transamination reactions. The addition of an amine group enhances the compound's reactivity with carboxylic acids, activated NHS esters, and other carbonyl groups.

Dnp-RPLALWRS TFA is a fluorescent peptide substrate designed specifically for human matrilysin (MMP-7). Upon enzymatic cleavage at the alanine-leucine bond, the release of the Dnp group alleviates fluorescence quenching, enabling real-time quantitative analysis of MMP-7 activity by enhancing tryptophan emission. This compound offers a sensitive and efficient method for kinetic studies and inhibitor screening.

H-GLU-AMC-OH is an amino acid derivative that serves as a fluorescent peptide substrate for measuring the enzymatic activity of aminopeptidase A.

Ac-DNLD-AMC is a fluorogenic caspase-3 substrate. Upon enzymatic cleavage by caspase-3, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify caspase-3 activity. AMC displays excitation emission maxima of 340-360 and 440-460 nm, respectively.

Z-(L-Arg)-AMC is a fluorogenic substrate for trypsin, cathepsin B, and cathepsin H.1,2Upon enzymatic cleavage by trypsin, cathepsin B, or cathepsin H, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify trypsin, cathepsin B, and cathepsin H activity. AMC displays excitation emission maxima of 340-360 440-460 nm, respectively. 1.Zimmerman, M., Ashe, B., Yurewicz, E.C., et al.Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substratesAnal. Biochem.78(1)47-51(1977) 2.Brindley, P.J., Kalinna, B.H., Dalton, J.P., et al.Proteolytic degradation of host hemoglobin by schistosomesMol. Biochem. Parasitol.89(1)1-9(1997)

L-Leu-AMC is a fluorogenic substrate for leucine aminopeptidase.1Upon enzymatic cleavage by leucine aminopeptidase, AMC is released and its fluorescence can be used to quantify leucine aminopeptidase activity. AMC displays excitation emission maxima of 340-360 440-460 nm, respectively. 1.Izquierdo, M., Lin, D., O'Neill, S., et al.Development of a high-throughput screening assay to identify inhibitors of the major M17-leucyl aminopeptidase from Trypanosoma cruzi using rapidfire mass spectrometrySLAS Discov.25(9)1064-1071(2020)

7-hydroxycoumarinyl-γ-Linolenate is a substrate for cytoplasmic phospholipase A2 (cPLA2), which shows cPLA2α enzymatic activity through hydrolysis of 7-hydroxycoumarinyl-γ-linolenate.

Thymolphthalein monophosphate disodium hydrate serves as a chromogenic substrate for the detection of acid phosphatase and alkaline phosphatase. During the enzymatic reaction, thymolphthalein is liberated which elevates the medium's pH, facilitating easy detection through color production and halts hydrolysis. Additionally, this compound is utilized for the specific identification of prostatic phosphatase in serum [1] [2].

AMCA-6-dUTP is suitable for the enzymatic labeling of DNA cDNA [1].

Mca-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 (FS-6) is a quenched, fluorescent MMP peptide substrate designed for real-time quantification of MMP enzymatic activity. As an extended variant of the MMP substrate (FS-1), it demonstrates increased specificity against collagenases (MMP-1, MMP-8, MMP-13) and MT1-MMP, with higher specificity constants (Ex Em=325 nm 400 nm). [1]

Dibenzylfluorescein (DBF), a fluorogenic probe (Fluorescent dye), serves as a substrate for various cytochrome P450 (CYP) isoforms, such as CYP3A4, CYP2C8, CYP2C9, CYP2C19, and aromatase (CYP19). It is commonly utilized at its K_m value range of 0.87-1.9 µM (Ex=485nm, Em=535nm) to monitor alterations in CYP enzymatic activity attributable to pharmaceutical interventions or pathophysiological conditions [1] [2] [3] [4].

Z-Gly-Pro-Arg-AMC hydrochloride is a synthetic peptide that is often used as a trypsin and histone K fluorescent substrate to measure enzyme activity, which fluoresces when the enzyme is cleaved from the peptide.

Prostate Specific Antigen Substrate is a fluorescent substrate specific to prostate-specific antigen (PSA), facilitating the detection of PSA enzymatic activity [1].

Purple-β-D-Gal, a chromogenic β-galactosidase substrate, undergoes enzymatic hydrolysis by intracellular β-galactosidase, yielding indoxyl molecules that oxidize and dimerize in situ to form water-insoluble indigo precipitates advantageous for β-galactosidase activity detection [1].

N-Acetyl-DL-phenylalanine β-naphthyl ester is a chromogenic substrate for chymotrypsin and microbial serine proteases like subtilisin [1]. This aromatic amino acid ester exhibits color changes upon enzymatic cleavage, facilitating the monitoring of enzyme activity.

Mca-SEVNLDAEFK(Dnp)-NH2 is a fluorogenic substrate featuring a 7-methoxycoumarin moiety whose fluorescence is quenched by the adjacent 2,4-dinitrophenyl group through resonance energy transfer. This compound serves as a probe for assessing peptidase activity; enzymatic cleavage of the amide bond separating the fluorophore and quencher results in increased fluorescence. It is particularly useful for quantifying the activity of BACE-1 [1].

BOD-NH-NP is a fluorescent probe designed for the specific detection of endogenous nitric oxide through the eNOS enzymatic pathway [1].

Biotin-PEG-Alk (MW 20000) is a biotin-labeled polyethylene glycol (PEG) derivative with a terminal alkyne group for efficient click chemistry applications. Biotin serves as an enzymatic cofactor, providing specific protein labeling, while the hydrophilic PEG moiety offers solubility and low toxicity. The alkyne functionality enables copper-catalyzed azide-alkyne cycloaddition (CuAAC), enhancing target binding through reaction with azide-modified molecules.