208721
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).
别名:
ALLM, Calpain Inhibitor II
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关于此项目
经验公式（希尔记法）:
C19H35N3O4S
化学文摘社编号:
分子量:
401.56
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.77
SMILES string
S(CC[C@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)C)CC(C)C)CC(C)C)C=O)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
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
Quality Level
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
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
Preparation Note
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Other Notes
N-Acetyl-Leu-Leu-Met
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.
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
Disclaimer
Toxicity: Standard Handling (A)
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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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