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).
Suberoylanilide hydroxamic acid (SAHA) is a class I and class II histone deacetylase (HDAC) inhibitor that binds directly to the catalytic site of the enzyme thereby blocking substrate access. [1] coumarin-Suberoylanilide hydroxamic acid (c-SAHA) is a SAHA derivative where the anilino cap group is replaced by 7-amino-4-methylcoumarin to produce a fluorescent probe that competitively binds HDAC. [2] The fluorescence excitation and emission maxima of free c-SAHA is 325 and 400 nm
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.
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.
Z-LLL-AMC is a fluorogenic substrate for the chymotrypsin-like activity of the 26S proteasome or 20S proteolytic core. Chymotrypsin-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-LLL-AMC is typically used in cell lysates after experimental treatment.
Ac-PAL-AMC is a fluorogenic substrate for the β1i LMP2 subunit of the 20S immunoproteasome. Upon cleavage, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify the activity of the β1i LMP2 subunit of the 20S immunoproteasome. Ac-PAL-AMC is selective for the immunoproteasome over the constitutive proteasome. AMC displays excitation emission maxima of 351 430 nm, respectively.