General description
Cell-permeable inhibitor of calpain I (Ki= 190 nM), calpain II (Ki= 220 nM), cathepsin B (Ki= 150 nM), and cathepsin L (Ki= 500 pM). Inhibits neutral cysteine proteases and the proteasome (Ki = 6 µM). Modulates the processing of the β-amyloid precursor protein (βAPP) to β-amyloid (Aβ). Protects against neuronal damage caused by hypoxia and ischemia. Inhibits apoptosis in thymocytes and metamyelocytes. Also inhibits reovirus-induced apoptosis in L929 cells. Inhibits the proteolysis of IκB-α and IκB-β by the ubiquitin-proteasome complex. Inhibits cell cycle progression at G₁/S and metaphase/anaphase in CHO cells by inhibiting cyclin B degradation. Also prevents nitric oxide production by activated macrophages by interfering with transcription of the inducible nitric oxide synthase gene. A 10 mM (5 mg/1.30 ml) solution of ALLN (Cat. No. 208750 ) in DMSO is also available.
Inhibitor of calpain I (Ki = 190 nM), calpain II (Ki = 220 nM), cathepsin B (Ki = 150 nM), and cathepsin L (Ki = 500 pM). Inhibits neutral cysteine proteases and proteasome (Ki = 6 µM). Protects against neuronal damage caused by hypoxia and ischemia. Inhibits apoptosis in thymocytes and metamyelocytes. Inhibits cell cycle progression at the G1/S border and metaphase/anaphase in CHO cells by inhibiting cyclin B degradation. Also prevents nitric oxide production by activated macrophages by interfering with transcription of the inducible nitric oxide synthase gene. Inhibits the proteolysis of IκBα and IκBβ by the ubiquitin-proteasome complex.
Biochem/physiol Actions
Cell permeable: yes
Primary Target
Calpain-1
Product does not compete with ATP.
Reversible: no
Target Ki: 190 nM, 220 nM, 150 nM, 500 pM, against calpain I, calpain II, cathepsin B, and cathepsin L, respectively
Preparation Note
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Other Notes
Debiasi, R.L., et al. 1999. J. Virol. 73, 695.
Zhang, L., et al. 1999. J. Biol. Chem.274, 8966.
Milligan, S.A., et al. 1996. Arch. Biochem. Biophys. 335, 388.
Griscavage, J.M., et al. 1995. Biochem. Biophys. Res. Commun. 215, 721.
Squier, M.K., et al. 1994. J. Cell Physiol.159, 229.
Rami, J., and Kreiglstein, J. 1993. Brain Res.609, 67.
Sherwood, S.W., et al. 1993. Proc. Natl. Acad. Sci.USA90, 3353.
Vinitsky, A., et al. 1992. Biochemistry31, 9421.
Sasaki, T., et al. 1990. J. Enzyme Inhib. 3, 195.
N-Acetyl-Leu-Leu-Nle-CHO
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
