General description
A cell-permeable, symmetrical bis(acylamino)ketone compound that acts as a potent, selective, reversible inhibitor of cathepsin K (Ki, = 22 nM). Also shown to inhibit cathepsin K in stably transfected CHO cells (IC50 = 134 nM). Reported to bind to cathepsin K and span both the S- and S′- subsites. Inhibits papain (Ki >10 µM), trypsin (Ki >50 µM), and chymotrypsin (Ki >50 µM) only at higher concentrations. Exhibits greater selectivity for cysteine proteases of the papain family (Ki = 340 nM, 890 nM, and 1-3 µM for cathepsin L, cathepsin S, and cathepsin B, respectively).
A cell-permeable, symmetrical bis(acylamino)ketone that acts as a potent, selective, and reversible inhibitor of cathepsin K (Ki,app = 22 nM). Shown to bind to cathepsin K and span both the S- and S′-subsites. A poor inhibitor of papain (Ki,app >10 µM) but displays greater selectivity towards other proteases of the papain family (Ki,app = 340 nM, 890 nM, and 1.3 µM for cathepsin L, cathepsin S, and cathepsin B respectively). Inhibits trypsin and chymotrypsin activities only at higher concentrations (Ki,app ≥ 50 µM).
Biochem/physiol Actions
Cell permeable: yes
Primary Target
cathepsin K
Product does not compete with ATP.
Reversible: yes
Target Ki: 22 nM against cathepsin K
Packaging
Packaged under inert gas
Warning
Toxicity: Standard Handling (A)
Sequence
Cbz-Leu-NH-CH₂-CO-CH₂-NH-Leu-Cbz
Reconstitution
Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Other Notes
Claveau, D., et al. 2000. Biochem. Pharmacol.60, 759.
LaLonde, J.M., et al. 1999. Biochemistry38, 862.
Yamashita, D.S., et al. 1997. J. Am. Chem. Soc.119, 11351.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
- UPC:
- 51282131
- Condition:
- New
- Weight:
- 1.00 Ounces
- HazmatClass:
- No
- WeightUOM:
- LB
- MPN:
- 219377-5MG