MMP-3 Inhibitor I

MMP-3 Inhibitor I is a synthetic research peptide in the matrix metalloproteinase fluorogenic peptide substrate family. Matrix metalloproteinases cleave defined peptide sequences and are frequently studied with fluorogenic substrates in which proteolysis separates a fluorophore from a quencher. Synthetic single-stranded and triple-helical peptide substrates have been used to quantify MMP-1, MMP-2, MMP-3, MMP-9, MMP-13, and related enzyme activities and to investigate collagenase/gelatinase substrate recognition.

• MMP activity assays
• fluorogenic protease measurements
• MMP inhibitor screening
• collagenase/gelatinase specificity studies

The exact sequence, reporter group, phosphorylation state, stereochemistry, and terminal modifications should be considered when comparing this reagent with the parent peptide or published assay substrates. Enzyme concentration, buffer composition, cofactors, pH, ionic strength, and substrate concentration can also affect measured activity.

1. Kinetic analysis of matrix metalloproteinase activity using fluorogenic triple-helical substrates
2. Detection of MMP-2 and MMP-9 activity with a triple-helical peptide optical probe