MMP-3 enzyme is also known as Stromelysin-1 or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL-1 beta.|Human recombinant 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. It has an MW of 52 kDa and has been purified by using proprietary chromatographic techniques.
Human MMP3 expressed in HEK cells
CAT# CSC-CTK0370-10 (10 μg); CAT# CSC-CTK0370-50 (50 μg)
Greater than 95% as determined by SDS-PAGE analysis.
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/μg.
Sterile-filtered (0.2 μm), colorless solution in Tris, NaCl and Brij35.
Please centrifuge product briefly before opening vial. The protein solution can be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid repeated freeze-thaw cycles.
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