ALLM

A cell-permeable inhibitor of calpain I (K_i = 120 nM), calpain II (K_i = 230 nM), cathepsin B (K_i = 100 nM), and cathepsin L (K_i = 0.6 nM). Inhibits activation-induced programmed cell death and restores defective immune responses in HIV⁺ donors. Also prevents nitric oxide produced by activated macrophages by interfering with transcription of the inducible nitric oxide synthase gene.

Cell permeable inhibitor of calpain I (K_i = 120 nM), calpain II (K_i = 230 nM), cathepsin B (K_i = 100 nM), and cathepsin L (K_i = 600 pM). Inhibits activation-induced programmed cell death and restores defective immune responses in HIV⁺ donors. Blocks nitric oxide production by activated macrophages by interfering with transcription of the inducible nitric oxide synthase gene. A weak inhibitor of proteasome.

Cell permeable: yes

Primary Target
calpain-1

Product does not compete with ATP.

Reversible: no

Target K_i: 120 nM, 230 nM, 100 nM, and 600 pM, against calpain I, calpain II, cathepsin B, and cathepsin L, respectively

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

N-Acetyl-Leu-Leu-Met

Ravid, T., et al. 2000. J. Biol. Chem.275, 35840.
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Sarin, A., et al. 1994. J. Immunol.153, 862.
Sarin, A., et al. 1993. J. Exp. Med. 178, 1693.
Banik, N.L., et al. 1992. Neurochem. Res.17, 797.
Koohmaraie, M. 1992. Biochemie74, 239.
Pinter, M., et al. 1992. Biochemistry31, 8201.
Shenoy, A.M., and Brahmi, Z. 1991. Cell. Immunol.138, 24.
Sasaki, T., et al. 1990. J. Enzyme Inhib.3, 195.

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

Toxicity: Standard Handling (A)