Matrix metalloproteinase (MMP) inhibitor profiling kit, fluorometric RED

The MMP inhibitor profiling kit, fluorometric (also known as fluorimetric) RED is a complete assay system designed to examine the specificity of inhibitors against a panel of ten matrix metalloproteinase enzymes, using a quenched fluorogenic substrate OMNIMMP^® RED: TQ3-GABA-Pro-Cha-Abu-Smc-His-Ala-Dab(6’-TAMRA)-Ala-Lys-NH₂ [TQ3=quencher; GABA=4-aminobutyric acid; Cha=L-cyclohexylalanine; Abu=2-aminobutyric acid; Smc=S-methyl-L-cysteine; Dab=2,4-diaminobutyric acid; 6’-TAMRA=6’-tetramethylrhodamine]. TAMRA fluorescence is thoroughly quenched by the TQ3 group until cleavage by MMPs separates the two moieties.

The assays are performed in a convenient 96-well microplate format.  The compound NNGH is also included as a prototypic control inhibitor.

The matrix metalloproteinases, or MMPs, are extracellular proteases that function at a neutral pH to cleave a wide variety of substrates. These include basement membrane and extracellular matrix components, growth and death factors, cytokines, and cell and matrix adhesion molecules. The broad range of substrate specificities and expression patterns of MMPs results in their involvement in many different processes, both normal and pathological. Aberrant expression has been noted in cancer, angiogenesis, arthritis, inflammation, periodontal disease, emphysema, multiple sclerosis, pre-eclampsia, and chronic wounds, among others. The general structure of an MMP protein consists of a pre domain to direct secretion from the cell, a pro domain, a catalytic domain, and a C-terminal hemopexin domain. The catalytic site involves a coordinately-bound zinc ion. The inactive, or zymogen, form of the enzyme is activated by disruption of one of the coordinate bonds, usually via proteolytic removal of the pro domain.