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Sigma-Aldrich

ALLM

Cell permeable inhibitor of calpain I (Ki = 120 nM), calpain II (Ki = 230 nM), cathepsin B (Ki = 100 nM), and cathepsin L (Ki = 600 pM).

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Synonym(s):
ALLM, Calpain Inhibitor II
Empirical Formula (Hill Notation):
C19H35N3O4S
CAS Number:
110115-07-6
Molecular Weight:
401.56

Quality Level

100

Assay

>95% (HPLC)

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

color

off-white

solubility

DMSO: 5 mg/mL
ethanol: 5 mg/mL
methanol: 5 mg/mL

shipped in

ambient

storage temp.

2-8°C

InChI

1S/C19H35N3O4S/c1-12(2)9-16(20-14(5)24)19(26)22-17(10-13(3)4)18(25)21-15(11-23)7-8-27-6/h11-13,15-17H,7-10H2,1-6H3,(H,20,24)(H,21,25)(H,22,26)/t15-,16-,17-/m0/s1

InChI key

RJWLAIMXRBDUMH-ULQDDVLXSA-N

General description

A cell-permeable inhibitor of calpain I (Ki = 120 nM), calpain II (Ki = 230 nM), cathepsin B (Ki = 100 nM), and cathepsin L (Ki = 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 (Ki = 120 nM), calpain II (Ki = 230 nM), cathepsin B (Ki = 100 nM), and cathepsin L (Ki = 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.

Biochem/physiol Actions

Cell permeable: yes
Primary Target
calpain-1
Product does not compete with ATP.
Reversible: no
Target Ki: 120 nM, 230 nM, 100 nM, and 600 pM, against calpain I, calpain II, cathepsin B, and cathepsin L, respectively

Warning

Toxicity: Standard Handling (A)

Sequence

N-Acetyl-Leu-Leu-Met

Reconstitution

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

Other Notes

Ravid, T., et al. 2000. J. Biol. Chem.275, 35840.
Griscavage, J.M., et al. 1995. Biochem. Biophys. Res. Commun.215, 721.
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.

Legal Information

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Simone Barbero et al.
Cancer research, 69(9), 3755-3763 (2009-04-23)
Caspase-8 is a proapoptotic protease that suppresses neuroblastoma metastasis by inducing programmed cell death. Paradoxically, caspase-8 can also promote cell migration among nonapoptotic cells; here, we show that caspase-8 can promote metastasis when apoptosis is compromised. Migration is enhanced by

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