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C0483

Sigma-Aldrich

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

≥95%, solid

Sinonimo/i:

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

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About This Item

Formula empirica (notazione di Hill):
C35H44N4O9
Peso molecolare:
664.75
Numero MDL:
MFCD01074989
Codice UNSPSC:
12352209
ID PubChem:
329774798
NACRES:
NA.77

Livello qualitativo

200

Saggio

≥95%

Stato

solid

Solubilità

DMSO: soluble

Temperatura di conservazione

−20°C

Stringa SMILE

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
FOYHOBVZPWIGJM-KCHLEUMXSA-N

Amino Acid Sequence

Z-Leu-Leu-Glu-AMC

Descrizione generale

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

Applicazioni

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.

Azioni biochim/fisiol

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

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

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Certificati d'analisi (COA)

Lot/Batch Number
SLCG3355
SLBS1467V
SLBN2972V
SLBJ0243V
SLBH0918V

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Sigma-Aldrich

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Sigma-Aldrich

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Sigma-Aldrich

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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
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
Aimee D Husom et al.
Archives of biochemistry and biophysics, 421(1), 67-76 (2003-12-18)
Myofibrillar protein degradation is mediated through the ubiquitin-proteasome pathway. To investigate if altered proteasome activity plays a role in age-related muscle atrophy, we examined muscle size and proteasome function in young and aged F344BN rats. Significant age-related muscle atrophy was
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)
Salyan Bhattarai et al.
Journal of autoimmunity, 75, 118-129 (2016-08-16)
Idiopathic inflammatory myopathies (IIMs) are diseases with muscle weakness, morphologically characterized by inflammatory infiltration and increased expression of MHC class I molecule on myofibers. Immunoproteasome, as a proteolytic complex that shapes the repertoire of antigenic peptides, has been previously demonstrated
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