fluorogenic

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.

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

4-Methylumbelliferyl-β-D-Glucopyranoside (4-MU-GLU) is used in the GCase activity assay based on the catalytic hydrolysis of 4-methylumbelliferyl β-D-glucopyranoside that releases the highly fluorescent 4-methylumbelliferyl (4-MU).

Maleimide (2,5-Pyrroledione) (2,5-Pyrroledone) is a new nanoparticle surface functional group which favors easy conjugation with cell penetration peptides. The conjugation is enabled via click chemistry to preserve its biofunctions.

2'-Fluorothymidine (2'-Deoxy-2'-fluoro-5-Methyluridine) belongs to the thymidine (TdR) and methyluridine isozymes and is a highly selective substrate for thymidine kinase type 2 (TK2).hCYP3A4 Fluorogenic substrate 2 is a chelator of thymidine and methyluridine.

ERAP1-IN-1 is an endoplasmic reticulum aminopeptidase 1 (ERAP1) inhibitor that allosterically activates ERAP1's hydrolysis of fluorogenic and chromogenic amino acid substrates, while competitively inhibiting its activity toward a nonamer peptide representative of physiological substrates.

Phe-Pro-Arg-PABA-Resorufin is a Chromogenic and fluorogenic peptide substrate for the highly sensitive detection of proteases in biological matrices. The substrate is also applicable to the sensitive detection of the thrombin inhibitor dabigatran in human

7-Lysylalanyl-4-methylcoumarinamide is a Fluorogenic substrate for dipeptidyl aminopeptidase.

Gly-Arg-AMC is a fluorogenic substrate for cathepsin C.1 Upon enzymatic cleavage by cathepsin C, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify cathepsin C activity. AMC displays excitation/emission maxima of 340-360/440-460 nm, respectively. |1. Rubach, J.K., Cui, G., Schneck, J.L., et al. The amino-acid substituents of dipeptide substrates of cathepsin C can determine the rate-limiting steps of catalysis. Biochemistry 51(38), 7551-7568 (2012).

Z-VAD-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.

Ac-LEHD-AMC is a fluorogenic substrate for caspase-9.[1] Upon cleavage by caspase-9, 7-amino-4-methylcoumarin (AMC) is released, and its fluorescence can be used to quantify caspase-9 activity. AMC displays excitation emission maxima of 340-360 440-460 nm, respectively.

Ac-VEID-AMC is a fluorogenic substrate based on the caspase-6 cleavage site in lamin A at amino acids VEID during apoptosis.1It has also been reported to be cleaved by related proteases, including caspase-8.2Caspase activity can be quantified by fluorescent detection of free AMC (also known as 7-amino-4-methylcoumarin), which is excited at 340-360 nm and emits at 440-460 nm. 1.Talanian, R.V., Quinlan, C., Trautz, S., et al.Substrate specificities of caspase family proteasesJ. Biol. Chem.272(15)9677-9682(1997) 2.Chae, H.J., Park, K.M., Lee, G.Y., et al.Je-Chun-Jun induced apoptosis of human cervical carcinoma HeLa cellsActa Pharmacologica Sinica25(10)1372-1379(2004)

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.

Dnp-P-Cha-G-Cys(Me)-HA-K(Nma)-NH2 is a fluorogenic substrate for matrix metalloproteinase-1 (MMP-1) and MMP-9. Upon cleavage by MMP-1 or MMP-9, N-methylanthranilic acid (Nma) is unquenched and its fluorescence can be used to quantify MMP activity. Nma displays excitation/emission spectra of 340/440 nm, respectively.

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.

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.

Dnp-RPLALWRS is a fluorogenic substrate for matrix metalloproteinase-7 (MMP-7). The activity of MMP-7 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group.

Ac-RGK(Ac)-AMC, fluorogenic substrate for assaying histone deacetylase (HDAC) activity in a two-step enzymatic reaction. The assay consists of the initial lysine deacetylation by HDAC followed by the release of the fluorescent group by trypsin.

Boc-LRR-AMC is a fluorogenic substrate for the trypsin-like activity of the 26S proteasome or 20S proteolytic core. Upon enzymatic cleavage by the 26S proteasome or 20S proteolytic core, amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify 26S proteasome or 20S proteolytic core trypsin-like activity. AMC displays excitation emission maxima of 340-360 440-460 nm, respectively.

Mu-6S-Palm-β-Glc is a fluorogenic substrate of palmitoyl-protein thioesterase (PPT, also known as CLN1), a lysosomal hydrolase that removes long-chain fatty acyl groups from modified cysteine residues in proteins. Upon cleavage by PPT CLN1, it releases 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. This substrate is used in assays measuring PPT activity, commonly deficient in the neurodegenerative disorder known as infantile neuronal ceroid lipofuscinosis.

4-Methylumbelliferyl-α-D-Galactopyranoside (4MU-α-Gal) (4-MU-α-Gal) is a fluorogenic substrate of α-galactosidase. In addition to its use in characterizing novel α-galactosidases, 4-MU-α-Gal is used in assays to evaluate deficiency in α-galactosidase activity related to Fabry disease.

4-Methylumbelliferyl-2-acetamido-2-deoxy-β-D-glucopyranoside is a fluorogenic substrate for β-hexosaminidases. Upon enzymatic cleavage by β-hexosaminidases, 4-methylumbelliferone (4-μU) is released, and its fluorescence quantifies β-hexosaminidase activity. 4-MU 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. This compound has been used to quantify β-hexosaminidase activity in serum or leukocytes from patients with GM2 gangliosidoses, such as Tay-Sachs disease, which is characterized by defects in the α subunit of β-hexosaminidase.

Z-LLE-AMC is a fluorogenic substrate for the caspase-like post-glutamate peptide hydrolase of the 26S proteasome or 20S proteolytic core. Caspase-like activity can be quantified by fluorescent detection of free AMC (also known as 7-amino-4-methylcoumarin), which is excited at 340-360 nm and emits at 440-460 nm. Z-LLE-AMC is typically used in cell lysates after experimental treatment.