Matrix Metalloproteinase 3, Recombinant, Human (MMP-3, Stromelysin-1, SL-1, Transin), M2421-12H-10ug

Matrix metalloproteinases are important regulators of extracellular matrix molecules and cell-cell signaling and are involved in the regulation of the pericellular space, including the cleavage of matrix proteins. In particular, MMP3 has been shown to be effective in cleaving heparan sulfate proteoglycans. Purified recombinant MMP3 can directly cleave agrin, and it can also remove agrin from synaptic basal lamina. MMP3 activity is itself regulated as activation of MMP3 is lost in denervated muscles. Recombinant Human MMP-3 produced in HEK293 cells is a proform of the Human MMP3 [Tyr18-Cys477 (Lys45Glu)] and fused with a his-tag at the C-terminus. Matrix Metalloproteinase-3 is purified by proprietary chromatographic techniques. Biological Activity: The activity was measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2. The specific activity is > 150 pmoles/min/ug. Storage and Stability: Lyophilized powder is stable for 12 months at -20°C Reconstituted product must be stored in aliquots at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.