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.
Commendamide (N-acyl-3-hydroxypalmitoyl-glycine) is a newly discovered GPCR G2A/GPR132 agonist (EC50=11.8 μM) that isolated from Bacteroides vulgatus. [1] G2A/GPR132 belongs to the guanine nucleotide-binding protein (G protein)-coupled receptor (GPCR) superfamily. GPR132/G2A is first reported to be a transcriptional target for BCR-ABL tyrosine kinase attenuating B-cell expansion in vitro and arresting cells at G2 during mitosis. It has been involved in autoimmune disease and atherosclerosis. [1] Commendamide and structurally related endogenous long-chain N-Acyl-amides activates discrete human receptors. In a screen for agonist activity against a library of 242 GPCRs, commendamide is found to activate a single receptor G2A/GPR132. This activity is confirmed by a synthetic sample of commendamide. Commendamide analogs with changes in the head group or acyl chain also exhibited reduced GPR132/G2A activity. [1]
Ac-DMQD-AMC, an inhibitor of caspase-3, is an aromatic amine synthesized using the aminium-based coupling reagent HATU in the presence of 2,4,6-trimethylpyridine (TMP) [1].
Substrate for dengue virus NS2B-NS3 and yellow fever virus NS3 protease. The kcat/Km value of Bz-NleKRR-AMC for the dengue virus type 4 (DEN4) enzyme is > 800 fold higher than that of Boc-Gly-Arg-Arg-AMC, a widely used NS3 substrate (kcat = 2.9 s 1, Km = 8.6 μM for DEN4). For yellow fever virus NS3 protease the kcat value was 0.111 s 1, the Km value 14.6 μM.
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.
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)
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.