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S6510

Sigma-Aldrich

N-Succinyl-Leu-Leu-Val-Tyr-7-Amido-4-Methylcoumarin

≥90% (HPLC)

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About This Item

Fórmula empírica (Notação de Hill):
C40H53N5O10
Número CAS:
94367-21-2
Peso molecular:
763.88
Número MDL:
MFCD00080248
Código UNSPSC:
12352200
ID de substância PubChem:
24899709
NACRES:
NA.77

Ensaio

≥90% (HPLC)

forma

powder

solubilidade

0.1% trifluoroacetic acid in acetonitrile: water (3:1): 1 mg/mL, clear, colorless

temperatura de armazenamento

−20°C

cadeia de caracteres SMILES

CC(C)CC(NC(=O)CCC(O)=O)C(=O)NC(CC(C)C)C(=O)NC(C(C)C)C(=O)NC(Cc1ccc(O)cc1)C(=O)Nc2ccc3C(C)=CC(=O)Oc3c2

InChI

1S/C40H53N5O10/c1-21(2)16-29(42-33(47)14-15-34(48)49)38(52)43-30(17-22(3)4)39(53)45-36(23(5)6)40(54)44-31(19-25-8-11-27(46)12-9-25)37(51)41-26-10-13-28-24(7)18-35(50)55-32(28)20-26/h8-13,18,20-23,29-31,36,46H,14-17,19H2,1-7H3,(H,41,51)(H,42,47)(H,43,52)(H,44,54)(H,45,53)(H,48,49)

chave InChI

UVFAEQZFLBGVRM-UHFFFAOYSA-N

Categorias relacionadas

Amino Acid Sequence

N-Suc-Leu-Leu-Val-Tyr-7-AMC

Aplicação

N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin was used in proteasome chymotrypsin-like activity assay in Jurkat cell lysate6 and crude cell lysate of rice.7

Ações bioquímicas/fisiológicas

In the presence of chymotrypsin-like enzyme activity, the fluorophore, 7-amido-4-methylcoumarin is released from N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin. The fluorescence obtained is a measure of the enzyme activity.6

Embalagem

Bottomless glass bottle. Contents are inside inserted fused cone.

Substratos

Fluorogenic substrate for chymotrypsin-like enzymes, such as cathepsin B and calpain which have been implicated in programmed cell death.

Frases de perigo

H413

Declarações de precaução

P273

Classificações de perigo

Aquatic Chronic 4

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)

Certificados de análise (COA)

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O Ullrich et al.
Proceedings of the National Academy of Sciences of the United States of America, 96(11), 6223-6228 (1999-05-26)
The 20S proteasome has been shown to be largely responsible for the degradation of oxidatively modified proteins in the cytoplasm. Nuclear proteins are also subject to oxidation, and the nucleus of mammalian cells contains proteasome. In human beings, tumor cells
S Glockzin et al.
The Journal of biological chemistry, 274(28), 19581-19586 (1999-07-03)
The ubiquitin/proteasome pathway mediates the degradation of many short-lived proteins that are critically involved in the regulation of cell proliferation and cell death, including the tumor suppressor protein p53. Accumulation of p53 and induction of apoptosis in RAW 264.7 macrophages
Miguel Díaz-Hernández et al.
Journal of neurochemistry, 98(5), 1585-1596 (2006-06-22)
In Huntington's disease (HD), as in the rest of CAG triplet-repeat disorders, the expanded polyglutamine (polyQ)-containing proteins form intraneuronal fibrillar aggregates that are gathered into inclusion bodies (IBs). Since IBs contain ubiquitin and proteasome subunits, it was proposed that inhibition
Madeline R Scott et al.
Molecular psychiatry, 25(4), 776-790 (2019-01-27)
Protein homeostasis is an emerging component of schizophrenia (SZ) pathophysiology. Proteomic alterations in SZ are well-documented and changes in transcript expression are frequently not associated with changes in protein expression in SZ brain. The underlying mechanism driving these changes remains
T Reinheckel et al.
Archives of biochemistry and biophysics, 377(1), 65-68 (2000-04-25)
The 20S proteasome and the 26S proteasome are major components of the cytosolic and nuclear proteasomal proteolytic systems. Since proteins are known to be highly susceptible targets for reactive oxygen species, the effect of H(2)O(2) treatment of K562 human hematopoietic
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