Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. The importance of MMPs in tumor development and invasion as well as other diseases is well known. MMP-3 (stromelysin-1, transin-1) has been shown to involved in tumor metastasis3 and rheumatoid arthritis. Therefore it is proposed as a therapeutic target for these diseases. The native pro-MMP-3 is Mr 59/57-kDa doublet, which can be autocatalyzed to an active form of 45-kDa, and is then processed partially to a second active form of 28-kDa.
Recombinant human MMP-3 enzyme was expressed as catalytic domain in E. coli. The molecular mass is 19.5 kDa. Purity is >95% by SDS-PAGE. Recombinant human MMP-3 catalytic domain doesn’t need APMA activation before enzyme assay. Its activity can be measured in FRET-based enzymatic assays.