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C0483

Sigma-Aldrich

Z-Leu-Leu-Glu-7-amido-4-methylcoumarin

≥95%, solid

Synonyme(s) :

Cbz-Leu-Leu-Glu-AMC, Z-LLE-AMC

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About This Item

Formule empirique (notation de Hill):
C35H44N4O9
Poids moléculaire :
664.75
Numéro MDL:
Code UNSPSC :
12352209
ID de substance PubChem :
Nomenclature NACRES :
NA.77

Niveau de qualité

Pureté

≥95%

Forme

solid

Solubilité

DMSO: soluble

Température de stockage

−20°C

Chaîne SMILES 

CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)Nc2ccc3C(C)=CC(=O)Oc3c2

InChI

1S/C35H44N4O9/c1-20(2)15-27(38-34(45)28(16-21(3)4)39-35(46)47-19-23-9-7-6-8-10-23)33(44)37-26(13-14-30(40)41)32(43)36-24-11-12-25-22(5)17-31(42)48-29(25)18-24/h6-12,17-18,20-21,26-28H,13-16,19H2,1-5H3,(H,36,43)(H,37,44)(H,38,45)(H,39,46)(H,40,41)/t26-,27-,28-/m0/s1

Clé InChI

FOYHOBVZPWIGJM-KCHLEUMXSA-N

Amino Acid Sequence

Z-Leu-Leu-Glu-AMC

Description générale

Z-Leu-Leu-Glu-7-amido-4-methylcoumarin is a fluoropeptide. It acts as a substrate for caspase-like activity.

Application

Z-Leu-Leu-Glu-7-amido-4-methylcoumarin has been used as a fluorogenic substrate for peptidyl glutamyl peptide hydrolase (PGPH) in rat soleus muscle, neonatal cardiomyocytes and rat brain samples.

Actions biochimiques/physiologiques

Fluorogenic substrate for the measurement of the peptidylglutamyl-peptide hydrolyzing activity of the 20S proteasome.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Caterina Branca et al.
Neurobiology of aging, 35(12), 2726-2735 (2014-07-19)
Currently, there are no available approaches to cure or slow down the progression of Alzheimer's disease (AD), which is characterized by the accumulation of extracellular amyloid-β (Aβ) deposits and intraneuronal tangles that comprised hyperphosphorylated tau. The β2 adrenergic receptors (β2ARs)
P Berthon et al.
Pflugers Archiv : European journal of physiology, 454(4), 625-633 (2007-03-06)
In the present study, we determined the impact of 5 and 10 days of muscle deconditioning induced by hindlimb suspension (HS) on the ubiquitin-proteasome system of protein degradation and caspase enzyme activities in rat soleus muscles. A second goal was
O I Savchuk et al.
Fiziolohichnyi zhurnal (Kiev, Ukraine : 1994), 61(5), 11-20 (2016-02-06)
Functional as well as structural reorganization of brain tissues takes place in the surrounding and remotes brain areas after focal ischemic lesions. In particular, reactive or regenerative processes have been described to occur in the infarction areas and the contralateral
M Orlowski et al.
Biochemistry, 32(6), 1563-1572 (1993-02-16)
Initial studies on the specificity of the multicatalytic proteinase complex (MPC; EC 3.4.99.46) led to the identification of three distinct proteolytic components designated as trypsin-like, chymotrypsin-like, and peptidylglutamyl-peptide hydrolyzing, all sensitive to inactivation by 3,4-dichloroisocoumarin (DCI), a general serine proteinase
Anita Swatek et al.
International journal of molecular sciences, 21(7) (2020-04-08)
The 26S proteasome is an ATP-dependent protease complex (2.5 MDa) that degrades most cellular proteins in Eukaryotes, typically those modified by a polyubiquitin chain. The proteasome-mediated proteolysis regulates a variety of critical cellular processes such as transcriptional control, cell cycle

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