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Leu-AMC [L-Leucine-7-amido-4-methylcoumarin] *CAS 62480-44-8*

L-Leucine-7-amido-4-methylcoumarin
L-Leucine-7-amido-4-methylcoumarin
L-Leucine-7-amido-4-methylcoumarin
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Physical properties
Molecular weight324.80
SolventDMSO
Spectral properties
Excitation (nm)341
Emission (nm)441
Storage, safety and handling
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure
UNSPSC12352200

OverviewpdfSDSpdfProtocol


See also: Coumarins
CAS
62480-44-8
Molecular weight
324.80
Excitation (nm)
341
Emission (nm)
441
Leu-AMC is a fluorogenic substrate for leucine aminopeptidase. Upon the hydrolysis by proteases, Leu-AMC releases the strongly fluorescent AMC fluorophore.

Calculators


Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of Leu-AMC [L-Leucine-7-amido-4-methylcoumarin] *CAS 62480-44-8* to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.

0.1 mg0.5 mg1 mg5 mg10 mg
1 mM307.882 µL1.539 mL3.079 mL15.394 mL30.788 mL
5 mM61.576 µL307.882 µL615.764 µL3.079 mL6.158 mL
10 mM30.788 µL153.941 µL307.882 µL1.539 mL3.079 mL

Molarity calculator

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Spectrum


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spectrum

Spectral properties

Excitation (nm)341
Emission (nm)441

Product Family


NameExcitation (nm)Emission (nm)
Pro-AMC341441
Ala-AMC341441

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References


View all 39 references: Citation Explorer
Molecular and biochemical characterization of methionine aminopeptidase of Babesia bovis as a potent drug target
Authors: Munkhjargal T, Ishizaki T, Guswanto A, Takemae H, Yokoyama N, Igarashi I.
Journal: Vet Parasitol (2016): 14
Secretory Expression, Purification, Characterization, and Application of an Aspergillus oryzae Prolyl Aminopeptidase in Bacillus subtilis
Authors: Wang KD, Wang KH, Zhou ND, Tian YP.
Journal: Appl Biochem Biotechnol. (2016)
Inhibition of leucine aminopeptidase 3 suppresses invasion of ovarian cancer cells through down-regulation of fascin and MMP-2/9
Authors: Wang X, Shi L, Deng Y, Qu M, Mao S, Xu L, Xu W, Fang C.
Journal: Eur J Pharmacol (2015): 116
Essential Role for an M17 Leucine Aminopeptidase in Encystation of Acanthamoeba castellanii
Authors: Lee YR, Na BK, Moon EK, Song SM, Joo SY, Kong HH, Goo YK, Chung DI, Hong Y.
Journal: PLoS One (2015): e0129884
Molecular Characterization of Babesia bovis M17 Leucine Aminopeptidase and Inhibition of Babesia Growth by Bestatin
Authors: Aboge GO, Cao S, Terkawi MA, Masatani T, Goo Y, AbouLaila M, Nishikawa Y, Igarashi I, Suzuki H, Xuan X.
Journal: J Parasitol (2015): 536
Modelling of human leucyl aminopeptidases for in silico off target binding analysis of potential Plasmodium falciparum leucine aminopeptidase (PfA-M17) specific inhibitors
Authors: Sahi S, Raj U, Chaudhary M, Nain V.
Journal: Recent Pat Endocr Metab Immune Drug Discov (2014): 191
Design, synthesis and preliminary activity evaluation of novel 3-amino-2-hydroxyl-3-phenylpropanoic acid derivatives as aminopeptidase N/CD13 inhibitors
Authors: Zhang X, Zhang L, Zhang J, Feng J, Yuan Y, Fang H, Xu W.
Journal: J Enzyme Inhib Med Chem (2013): 545
Novel leucine ureido derivatives as inhibitors of aminopeptidase N (APN)
Authors: Ma C, Jin K, Cao J, Zhang L, Li X, Xu W.
Journal: Bioorg Med Chem (2013): 1621
The Staphylococcus aureus leucine aminopeptidase is localized to the bacterial cytosol and demonstrates a broad substrate range that extends beyond leucine
Authors: Carroll RK, Veillard F, Gagne DT, Lindenmuth JM, Poreba M, Drag M, Potempa J, Shaw LN.
Journal: Biol Chem (2013): 791
Enzymatic and molecular characterisation of leucine aminopeptidase of Burkholderia pseudomallei
Authors: Liew SM, Tay ST, Puthucheary SD.
Journal: BMC Microbiol (2013): 110