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Ac-YVAD-AFC is a substrate whose amino acids YVAD have been shown to be a preferred cleavage site for caspase-1 and -4. Caspase activity can be quantified by fluorescent detection of free AFC (also known as 7-amino-4-trifluoromethylcoumarin), which is excited at 400 nm and emits at 505 nm.

N-Acetyl-Tyr-Val-Ala-Asp-7-amido-4-trifluoromethylcoumarin is a substrate whose amino acids are shown as a preferred cleavage site for Caspase-1 and 4. Useful for caspase research.

ChEBI: Ac-Tyr-Val-Ala-Asp-7-amino-4-trifluoromethylcoumarin is a tetrapeptide obtained by formal condensation of the C-terminal carboxy group of Ac-Tyr-Val-Ala-Asp with the amino group of 7-amino-4-trifluoromethylcoumarin. It has a role as a protease inhibitor. It is a tetrapeptide, a member of acetamides, a member of coumarins and an organofluorine compound. It is functionally related to a 7-amino-4-(trifluoromethyl)coumarin.

Fluorogenic peptide substrate for caspase-1 (ICE).

[1] R V TALANIAN. Substrate specificities of caspase family proteases.[J]. The Journal of Biological Chemistry, 1997, 272 15: 9677-9682. DOI: 10.1074/jbc.272.15.9677
[2] M MARCELLI. Caspase-7 is activated during lovastatin-induced apoptosis of the prostate cancer cell line LNCaP.[J]. Cancer research, 1998, 58 1: 76-83.