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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).

Synonyme(s) :

ALLM, Calpain Inhibitor II

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About This Item

Formule empirique (notation de Hill):
C19H35N3O4S
Numéro CAS:
Poids moléculaire :
401.56
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.77

Niveau de qualité

Pureté

>95% (HPLC)

Forme

solid

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze

Couleur

off-white

Solubilité

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

Conditions d'expédition

ambient

Température de stockage

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

Clé InChI

RJWLAIMXRBDUMH-ULQDDVLXSA-N

Description générale

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.

Actions biochimiques/physiologiques

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

Avertissement

Toxicity: Standard Handling (A)

Séquence

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.

Autres remarques

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.

Informations légales

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°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

Contenu apparenté

Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

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