Cathepsin K Inhibitor I-Calbiochem

C₃₁H₄₂N₄O₇

582.69

A cell-permeable, symmetrical bis(acylamino)ketone that acts as a potent, selective, and reversible inhibitor of cathepsin K (K_i,app = 22 nM). Shown to bind to cathepsin K and span both the S- and S′-subsites. A poor inhibitor of papain (K_i,app >10 µM) but displays greater selectivity towards other proteases of the papain family (K_i,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 (K_i,app ≥ 50 µM).
A cell-permeable, symmetrical bis(acylamino)ketone compound that acts as a potent, selective, reversible inhibitor of cathepsin K (K_i, = 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 (K_i >10 µM), trypsin (K_i >50 µM), and chymotrypsin (K_i >50 µM) only at higher concentrations. Exhibits greater selectivity for cysteine proteases of the papain family (K_i = 340 nM, 890 nM, and 1-3 µM for cathepsin L, cathepsin S, and cathepsin B, respectively).

Primary Target
cathepsin K
Product does not compete with ATP.
Reversible: yes
Cell permeable: yes
Target K_i: 22 nM against cathepsin K

Toxicity: Standard Handling (A)

Cbz-Leu-NH-CH₂-CO-CH₂-NH-Leu-Cbz

Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.

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.

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

100

≥95% (HPLC)

lyophilized solid

Calbiochem^®

OK to freeze

off-white

methanol: 1 mg/mL
DMSO: soluble

wet ice

−20℃

5 mg in Plastic ampoule
Packaged under inert gas

11 - Combustible Solids

WGK 1