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.
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.
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
- UPC:
- 12352200
- Condition:
- New
- Weight:
- 1.00 Ounces
- HazmatClass:
- No
- WeightUOM:
- LB
- MPN:
- 444274-500UG