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Merck
CN

64367

L-Methionine 7-amido-4-methylcoumarin trifluoroacetate salt

≥99.0% (sum of enantiomers, HPLC)

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About This Item

Empirical Formula (Hill Notation):
C15H18N2O3S · C2HF3O2
CAS Number:
94367-35-8
Molecular Weight:
420.40
NACRES:
NA.32
PubChem Substance ID:
57651980
UNSPSC Code:
12352209
MDL number:
MFCD00210065

Key Documents

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Product Name

L-Methionine 7-amido-4-methylcoumarin trifluoroacetate salt, ≥99.0% (sum of enantiomers, HPLC)

InChI key

VSAUWUJWXBUSEU-YDALLXLXSA-N

SMILES string

OC(=O)C(F)(F)F.CSCC[C@H](N)C(=O)Nc1ccc2C(C)=CC(=O)Oc2c1

InChI

1S/C15H18N2O3S.C2HF3O2/c1-9-7-14(18)20-13-8-10(3-4-11(9)13)17-15(19)12(16)5-6-21-2;3-2(4,5)1(6)7/h3-4,7-8,12H,5-6,16H2,1-2H3,(H,17,19);(H,6,7)/t12-;/m0./s1

assay

≥99.0% (sum of enantiomers, HPLC)

optical activity

[α]20/D +68±3°, c = 1% in methanol

storage temp.

2-8°C

Quality Level

100

Application

L-Methionine 7-amido-4-methylcoumarin trifluoroacetate and its analogues may be used to study the kinetics of methionine aminopeptidase (hMetAP2). L-Methionine 7-amido-4-methylcoumarin trifluoroacetate may be use with other substrates to assess the specificity of various aminopeptidases.

Other Notes

Substrate for calpain

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
BCCM8049
BCCD9523
BCCB8298
1260416
339781/1

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Gabriel Rinaldi et al.
Molecular and biochemical parasitology, 167(2), 118-126 (2009-05-26)
Schistosoma mansoni leucine aminopeptidase (LAP) is thought to play a central role in hatching of the miracidium from the schistosome egg. We identified two discrete LAPs genes in the S. mansoni genome, and their orthologs in S. japonicum. The similarities
G Yang et al.
Biochemistry, 40(35), 10645-10654 (2001-08-29)
The steady-state kinetics of a full-length and truncated form of the type 2 human methionine aminopeptidase (hMetAP2) were analyzed by continuous monitoring of the amide bond cleavage of various peptide substrates and methionyl analogues of 7-amido-4-methylcoumarin (AMC) and p-nitroaniline (pNA)
T Sasaki et al.
The Journal of biological chemistry, 259(20), 12489-12494 (1984-10-25)
Homogeneous porcine calpain (Ca2+-dependent cysteine proteinase) was found to hydrolyze a variety of peptides and synthetic substrates. Leu-Trp-Met-Arg-Phe-Ala, eledoisin-related peptide, alpha-neoendorphin, angiotensin I, luteinizing hormone-releasing hormone, neurotensin, dynorphin, glucagon, and oxidized insulin B chain were cleaved with a general preference

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