85-1451-49　Matrix Metalloproteinase 3, Recombinant, Human (MMP-3, Stromelysin-1, SL-1, Transin) 10ug　M2421-12H

特徴

• 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 ployhistide tag at the C-terminus, having an Mw of 52kD. 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 >150pmoles/min/ug
• Recombinant Human MMP-3 protein pro form needs to be activated with Chymotrypsin.
• Activation Protocol:1. Dilute MMP3 to 20µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM sodium chloride, 0.05%and Brij 35, pH 7.5
• 2. Activate MMP3 by adding Chymotrypsin to a final concentration of 5ug/ml
• 3. Incubate at 37°C for 30 minutes
• 4. Stop activation with 2mM PMSF. Pre-warm the PMSF to 37°C prior to adding to sample.
• Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 6 months after receipt 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.