boclys(ac)amc

Ac-Lys-AMC (Hexanamide) is a fluorescent substrate for histone deacetylase HDACs.

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-Leu-Arg-AMC is a fluorogenic peptide substrate.

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-Trp-Glu-His-Asp-AMC (AC-WEHD-AMC) is a potent fluorogenic substrate of caspase-1 [1] .

Ac-DEVD-AMC (AC-ASP-MET-GLN-ASP-7-AMINO-4-METHYLCOUMARIN) is the substrate of Caspase-3 .

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-Nle-Pro-Nle-Asp-AMC is a specific substrate for the 26S proteasome and is utilized in analyzing the proteasome's caspase-like activity [1] [2] [3].

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.

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)