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Merck

A6185

Sigma-Aldrich

Calpain Inhibitor I

≥97% (TLC), powder

Sinónimos:

ALLN, Ac-LLnL-CHO, MG-101, N-Acetyl-L-leucyl-L-leucyl-L-norleucinal, N-Acetyl-Leu-Leu-Norleu-al

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About This Item

Fórmula empírica (notación de Hill):
C20H37N3O4
Número de CAS:
Peso molecular:
383.53
Beilstein/REAXYS Number:
7656053
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
NACRES:
NA.77

biological source

synthetic (organic)

Quality Level

assay

≥97% (TLC)

form

powder

color

white

solubility

DMSO: soluble
ethanol: soluble

storage temp.

−20°C

SMILES string

[H]C(=O)[C@H](CCCC)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(C)=O

InChI

1S/C20H37N3O4/c1-7-8-9-16(12-24)22-19(26)18(11-14(4)5)23-20(27)17(10-13(2)3)21-15(6)25/h12-14,16-18H,7-11H2,1-6H3,(H,21,25)(H,22,26)(H,23,27)/t16-,17-,18-/m0/s1

InChI key

FMYKJLXRRQTBOR-BZSNNMDCSA-N

Gene Information

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Application

Calpain Inhibitor I have been used:
  • as a component of protease inhibitor cocktail for gel shift analysis
  • for treating HeLa cell cultures
  • for inhibition of 26 S proteasome in 26 S proteasome inhibition assays

Biochem/physiol Actions

Calpain Inhibitor I inhibits tumor necrosis factor-induced (TNF-induced) cleavage of Poly (ADP-ribose) polymerase (PARP) and calpastatin in apoptosis. It also inhibits oxygen/glucose deprivation (OGD) induced cleavage of caspase-12 and Bcl-xL..
Can initiate apoptosis in HL-60 cells but blocks dexamethasone-induced apoptosis in thymocytes and cycloheximide-induced apoptosis in metamyelocytes. Inhibits cyclin B degradation and arrests the cell cycle at G1/S and at meta-/anaphase. Blocks induction of nitric oxide synthase by LPS in macrophages.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Los clientes también vieron

M K Squìer et al.
Journal of cellular physiology, 159(2), 229-237 (1994-05-01)
Programmed cell death is an active process wherein the cell initiates a sequence of events culminating in the fragmentation of its DNA, nuclear collapse, and disintegration of the cell into small, membrane-bound apoptotic bodies. Examination of the death program in
CRM1-mediated nuclear export is required for 26 S proteasome-dependent degradation of the TRIP-Br2 proto-oncoprotein
Cheong J K, et al.
The Journal of Biological Chemistry, 283(17), 11661-11676 (2008)
Cross-talk between two cysteine protease families: activation of caspase-12 by calpain in apoptosis
Nakagawa T and Yuan J
The Journal of Cell Biology, 150(4), 887-894 (2000)
Q Lu et al.
Archives of biochemistry and biophysics, 334(1), 175-181 (1996-10-01)
Recent investigations indicate that proteolysis is an important event in generation of the apoptosis phenotype. Although various proteases have been suggested to be candidates for this proteolysis, the results from different laboratories are inconsistent. In the present studies, HL-60 cells
S W Sherwood et al.
Proceedings of the National Academy of Sciences of the United States of America, 90(8), 3353-3357 (1993-04-15)
The cytotoxic neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal (ALLN) inhibits cell-cycle progression in CHO cells, affecting the G1/S and metaphase-anaphase transition points, as well as S phase. Mitotic arrest induced by ALLN is associated with the inhibition of cyclin B degradation.

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