Description General description A potent, selective, slow-binding and mechanism-based inhibitor of human gelatinases, MMP-2 (Ki = 13.9 nM) and MMP-9 (Ki = 600 nM). It also exhibits a covalent mechanism based behavior in inhibition of these enzymes. This inhibitor appears to have similarity to TIMP-1 and TIMP-2 in the slow-binding component of inhibition. Shown to directly bind to the zinc in the catalytic site of MMP-2. Does not affect the activities of MMP-1 (Ki = 206 µM) MMP-3 (Ki = 15 µM), or MMP-7 (Ki = 96 µM). A potent, selective, slow-binding and mechanism-based inhibitor of human gelatinases, MMP-2 (Ki = 13.9 nM), and MMP-9 (Ki = 600 nM). This inhibitor appears to behave similarly to TIMP-1 and TIMP-2 in the slow-binding component of inhibition. Also exhibits a covalent mechanism-based behavior in inhibition of these enzymes. Binds directly to the catalytic zinc ion on MMP-2. Packaging 500 μg in Plastic ampoule Biochem/physiol Actions Cell permeable: no Product does not compete with ATP. Reversible: no Packaging Packaged under inert gas Warning Toxicity: Standard Handling (A) Other Notes Krüger, A., et al. 2005. Cancer Res.65, 3523. Kleinfeld, O., et al. 2001. J. Biol. Chem.276, 17125. Brown, S., et al. 2000. J. Am. Chem. Soc.122, 6799. Legal Information Sold under license of U.S. Patent 6,703,415.