AAT Bioquest

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

Ordering information
Catalog Number
Unit Size
Add to cart
Additional ordering information
InternationalSee distributors
Bulk requestInquire
Custom sizeInquire
ShippingStandard overnight for United States, inquire for international
Request quotation
Physical properties
Molecular weight324.80
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


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


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

Enter any two values (mass, volume, concentration) to calculate the third.

Mass (Calculate)Molecular weightVolume (Calculate)Concentration (Calculate)Moles


Open in Advanced Spectrum Viewer

Spectral properties

Excitation (nm)341
Emission (nm)441

Product Family

NameExcitation (nm)Emission (nm)



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