Human MMP-3 - 100 µL

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

Human MMP-3 catalytic domain was expressed as 253 amino acid sequence (Pro19-Glu271) in E. coli. The molecular mass is approximately 28/29 kDa on SDS-PAGE. Recombinant human MMP-3 enzyme has catalytic domain only and doesn’t need APMA activation before enzyme assay. Its activity can be measured in FRET-based enzymatic assays

Specifications

Downloads