Enteropeptidase fluorogenic substrate is a substrate for enteropeptidase that contains a 7-amino-4-trifluoromethylcoumarin (AFC) moiety. Enteropeptidase is a serine protease expressed in the proximal small intestine of higher animals that converts inactive trypsinogen to active trypsin by endoproteolytic cleavage.1,2Enteropeptidase recognizes the highly specific amino acid sequence DDDDK on the fluorogenic substrate and cleaves after the lysine residue, releasing the AFC moiety. Enteropeptidase activity is quantified by fluorescent detection of AFC, which displays excitation/emission spectra of 380/500 nm.3
The renin fluorogenic substrate consists of the normal peptide substrate for renin which has been linked to the fluorophore EDANS at one end and to a non-fluorescent quenching molecule (Dabcyl) at the other. After cleavage by renin, the product (peptide-EDANS) is brightly fluorescent and can be easily analyzed using an excitation wavelength of 340 nm and emission wavelengths of 485-510 nm.
Enteropeptidase fluorogenic substrate is a substrate for enteropeptidase that contains a 7-amino-4-trifluoromethylcoumarin (AFC) moiety. Enteropeptidase is a serine protease expressed in the proximal small intestine of higher animals that converts inactive trypsinogen to active trypsin by endoproteolytic cleavage. Enteropeptidase recognizes the highly specific amino acid sequence DDDDK on the fluorogenic substrate and cleaves after the lysine residue, releasing the AFC moiety. Enteropeptidase activity is quantified by fluorescent detection of AFC, which displays excitation emission spectra of 380 500 nm.
BOP-JF549 is a fluorescent dual α9β1 α4β1 integrin inhibitor. Comprises BOP conjugated to Janelia Fluor® 549. Fluorogenic: fluoresces only once bound to integrins, enabling hassle-free no-wash experiments. Bright and photostable, enabling live cell tracking of integrin receptors over long time-course experiments. Excitation maximum = 549 nm; emission maximum = 571 nm.
Dnp-PLGMWSR is a fluorogenic substrate for matrix metalloproteinase-2 (MMP-2) and MMP-9. The activity of MMP-2 and MMP-9 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group.
4-Methylumbelliferyl caprylate (MUCAP) is a fluorogenic substrate for C8 esterase. MUCAP is cleaved by C8 esterase to release the fluorescent moiety 4-methylumbelliferyl (4-MU). 4-MU fluorescence is pH-dependent with excitation maxima of 320 and 360 nm at low (1.97-6.72) and high (7.12-10.3) pH, respectively, and an emission maximum ranging from 445 to 455 nm, increasing as pH decreases.
Dnp-PLALWAR is a fluorogenic substrate for matrix metalloproteinase-1 (MMP-1) and MMP-8. The activity of MMP-1 and MMP-8 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group.
4-Methylumbelliferyl β-D-N,N'-diacetylchitobioside (4-μU-(GlcNAc)2) is a fluorogenic substrate for chitinases and chitobiosidases. 4-μU-(GlcNAc)2 is cleaved by chitinases and chitobiosidases to release the fluorescent moiety 4-μU. 4-μU fluorescence is pH-dependent with excitation maxima of 320 and 360 nm at low (1.97-6.72) and high pH (7.12-10.3), respectively, and an emission maximum ranging from 445 to 455 nm, increasing as pH decreases.
BOP-JF646 is a fluorescent dual α9β1/α4β1 integrin inhibitor. Comprises BOP conjugated to Janelia Fluor®646. Fluorogenic: fluoresces only once bound to integrins, enabling hassle-free no-wash experiments. Bright and photostable, enabling live cell tracking of integrin receptors over long time-course experiments. Excitation maximum = 655 nm; emission maximum = 672 nm.
Suc-YVAD-AMC is a fluorogenic substrate for caspase-1. Upon enzymatic cleavage by caspase-1, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify caspase-1 activity. AMC displays excitation/emission maxima of 340-360/440-460 nm, respectively.