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Ac-Leu-AMC
Ordering information
| Price | |
| Catalog Number | |
| Unit Size | |
| Quantity |
Additional ordering information
| Telephone | 1-800-990-8053 |
| Fax | 1-800-609-2943 |
| sales@aatbio.com | |
| International | See distributors |
| Bulk request | Inquire |
| Custom size | Inquire |
| Shipping | Standard overnight for United States, inquire for international |
Physical properties
| Molecular weight | 330.38 |
| Solvent | DMSO |
Spectral properties
| Excitation (nm) | 341 |
| Emission (nm) | 441 |
Storage, safety and handling
| H-phrase | H303, H313, H333 |
| Hazard symbol | XN |
| Intended use | Research Use Only (RUO) |
| R-phrase | R20, R21, R22 |
| Storage | Freeze (< -15 °C); Minimize light exposure |
| Overview |  SDSProtocol |
Molecular weight 330.38 | Excitation (nm) 341 | Emission (nm) 441 |
Ac-Leu-AMC is a fluorogenic substrate for leucine aminopeptidase. Upon the hydrolysis by proteases, Leu-AMC releases the strongly fluorescent AMC fluorophore that can be readily detected with Ex/Em = 350/430 nm. Leucine aminopeptidase is an extracellular enzyme found abundantly in natural aquatic systems. It is one of the various enzymes used by bacteria for protein hydrolysis. Ac-L-Leucine-7-amido-4-methylcoumarin might be used as a substrate in fluorescence-based soil assays to determine leucine aminopeptidase activity of both Plasmodium falciparum M1 (PfA-M1) and PfA-M17 enzymes.
Calculators
Common stock solution preparation
Table 1. Volume of DMSO needed to reconstitute specific mass of Ac-Leu-AMC to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.
| 0.1 mg | 0.5 mg | 1 mg | 5 mg | 10 mg | |
| 1 mM | 302.682 µL | 1.513 mL | 3.027 mL | 15.134 mL | 30.268 mL |
| 5 mM | 60.536 µL | 302.682 µL | 605.364 µL | 3.027 mL | 6.054 mL |
| 10 mM | 30.268 µL | 151.341 µL | 302.682 µL | 1.513 mL | 3.027 mL |
Molarity calculator
Enter any two values (mass, volume, concentration) to calculate the third.
| Mass (Calculate) | Molecular weight | Volume (Calculate) | Concentration (Calculate) | Moles | ||||
| / | = | x | = |
Product Family
| Name | Excitation (nm) | Emission (nm) |
| Ac-DEVD-AMC *CAS 169332-61-0* | 341 | 441 |
| Ac-IETD-AMC | 341 | 441 |
| Ac-LEHD-AMC *CAS 292633-16-0* | 341 | 441 |
| Ac-LKKR-AMC | 341 | 441 |
Images
Figure 1. Ac-Leu-AMC is a fluorogenic substrate for leucine aminopeptidase. Upon the hydrolysis by proteases, Leu-AMC releases the strongly fluorescent AMC fluorophore that can be readily detected with Ex/Em = 350/430 nm.
References
View all 9 references: Citation Explorer
The Biochemical and Functional Characterization of M28 Aminopeptidase Protein Secreted by Acanthamoeba spp. on Host Cell Interaction.
Authors: Huang, Jian-Ming and Chang, Yao-Tsung and Lin, Wei-Chen
Journal: Molecules (Basel, Switzerland) (2019)
Authors: Huang, Jian-Ming and Chang, Yao-Tsung and Lin, Wei-Chen
Journal: Molecules (Basel, Switzerland) (2019)
Skeletocutins M-Q: biologically active compounds from the fruiting bodies of the basidiomycete Skeletocutis sp. collected in Africa.
Authors: Cheng, Tian and Chepkirui, Clara and Decock, Cony and Matasyoh, Josphat C and Stadler, Marc
Journal: Beilstein journal of organic chemistry (2019): 2782-2789
Authors: Cheng, Tian and Chepkirui, Clara and Decock, Cony and Matasyoh, Josphat C and Stadler, Marc
Journal: Beilstein journal of organic chemistry (2019): 2782-2789
Structural and functional highlights of methionine aminopeptidase 2 from Leishmania donovani.
Authors: Bhat, Saleem Yousuf and Dey, Arijit and Qureshi, Insaf A
Journal: International journal of biological macromolecules (2018): 940-954
Authors: Bhat, Saleem Yousuf and Dey, Arijit and Qureshi, Insaf A
Journal: International journal of biological macromolecules (2018): 940-954
Discovery of a pyruvylated peptide-metabolizing enzyme using a fluorescent substrate-based protein discovery technique.
Authors: Yoshioka, Kentaro and Komatsu, Toru and Hanaoka, Kenjiro and Ueno, Tasuku and Terai, Takuya and Nagano, Tetsuo and Urano, Yasuteru
Journal: Chemical communications (Cambridge, England) (2016): 4377-80
Authors: Yoshioka, Kentaro and Komatsu, Toru and Hanaoka, Kenjiro and Ueno, Tasuku and Terai, Takuya and Nagano, Tetsuo and Urano, Yasuteru
Journal: Chemical communications (Cambridge, England) (2016): 4377-80
A quantitative technique for determining proteases and their substrate specificities and pH optima in crude enzyme extracts.
Authors: Budic, Maruska and Kidric, Marjetka and Meglic, Vladimir and Cigić, Blaz
Journal: Analytical biochemistry (2009): 56-62
Authors: Budic, Maruska and Kidric, Marjetka and Meglic, Vladimir and Cigić, Blaz
Journal: Analytical biochemistry (2009): 56-62
Fasciola hepatica leucine aminopeptidase, a promising candidate for vaccination against ruminant fasciolosis.
Authors: Acosta, Daniel and Cancela, Martín and Piacenza, Lucia and Roche, Leda and Carmona, Carlos and Tort, José F
Journal: Molecular and biochemical parasitology (2008): 52-64
Authors: Acosta, Daniel and Cancela, Martín and Piacenza, Lucia and Roche, Leda and Carmona, Carlos and Tort, José F
Journal: Molecular and biochemical parasitology (2008): 52-64
Purification and properties of an arginyl aminopeptidase from Debaryomyces hansenii.
Authors: Bolumar, Tomás and Sanz, Yolanda and Aristoy, M-Concepción and Toldrá, Fidel
Journal: International journal of food microbiology (2003): 141-51
Authors: Bolumar, Tomás and Sanz, Yolanda and Aristoy, M-Concepción and Toldrá, Fidel
Journal: International journal of food microbiology (2003): 141-51
Comparison of different peptidase substrates for evaluation of microbial quality of aerobically stored meats.
Authors: Stepaniak, L
Journal: Journal of food protection (2000): 1447-9
Authors: Stepaniak, L
Journal: Journal of food protection (2000): 1447-9
HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome.
Authors: Rohrwild, M and Coux, O and Huang, H C and Moerschell, R P and Yoo, S J and Seol, J H and Chung, C H and Goldberg, A L
Journal: Proceedings of the National Academy of Sciences of the United States of America (1996): 5808-13
Authors: Rohrwild, M and Coux, O and Huang, H C and Moerschell, R P and Yoo, S J and Seol, J H and Chung, C H and Goldberg, A L
Journal: Proceedings of the National Academy of Sciences of the United States of America (1996): 5808-13