Ac-YEVD-AMC is a fluorogenic YEVD peptide substrate used in caspase-1/ICE activity studies. The tetrapeptide recognition sequence is linked to 7-amino-4-methylcoumarin for fluorescence-based detection after enzymatic cleavage.

YEVD provides an alternative inflammatory-caspase substrate motif to YVAD and can be useful when researchers are comparing sequence-dependent protease recognition.

Product Information

YEVD Sequence Recognition

Substrate profiling studies have shown that caspase-family enzymes distinguish peptide sequences through residues positioned upstream of the cleavage-site Asp. YEVD is efficiently processed by caspase-1 in established peptide-substrate systems.

The glutamate at the P3 position gives YEVD a different recognition profile from YVAD, making the two substrates useful for comparative biochemical experiments.

AMC-Based Detection

Proteolytic cleavage liberates AMC, generating a fluorescence signal suitable for continuous or endpoint analysis.

We recommend optimizing substrate concentration rather than assuming that assay conditions established for YVAD-AMC will transfer unchanged to YEVD-AMC.

Experimental Use

Ac-YEVD-AMC can be used in purified-enzyme studies, inflammatory caspase profiling and assay-development projects where fluorescence sensitivity is preferred.

Researchers developing modified protease substrates can explore our Chemical Peptide Synthesis capabilities.

Frequently Asked Questions

How does YEVD differ from YVAD?

YEVD contains glutamate at the third residue of the tetrapeptide sequence where YVAD contains alanine, changing the recognition environment presented to the protease.

What is the fluorescent reporter?

The reporter group is AMC, which becomes strongly fluorescent after release from the peptide.

Can YEVD-AMC be used as absolute proof of caspase-1 activity?

No. Substrate cleavage should be interpreted together with the enzyme composition and appropriate biological controls.

Research Use Only.