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Beta-Ala-AMC

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Physical properties
Molecular weight282.72
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
UNSPSC12171501

OverviewpdfSDSpdfProtocol


See also: Proteases
Molecular weight
282.72
Excitation (nm)
341
Emission (nm)
441
Beta-Ala-AMC is a fluorogenic substrate that might be used for detection pancreatic elastase, arylamidase and beta-alanine aminopeptidase activities. It may also be used for detecting Pseudomonas aeruginosa that have beta-alanine aminopeptidase activity. Beta-alanine aminopeptidase activity was detected in Serratia liquefaciens, Pseudomonas aeruginosa, Pseudomonas fluorescens, Burkholderia cepacia, Pseudomonas mendocina and Ochrobactrum anthropi. Therefore, beta-Ala-AMC may be used for detecting these species in food and other samples.

Calculators


Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of Beta-Ala-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 mg0.5 mg1 mg5 mg10 mg
1 mM353.707 µL1.769 mL3.537 mL17.685 mL35.371 mL
5 mM70.741 µL353.707 µL707.414 µL3.537 mL7.074 mL
10 mM35.371 µL176.853 µL353.707 µL1.769 mL3.537 mL

Molarity calculator

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

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Spectrum


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spectrum

Spectral properties

Excitation (nm)341
Emission (nm)441

Product Family


NameExcitation (nm)Emission (nm)Extinction coefficient (cm -1 M -1)
D-Ala-AMC *CAS 201847-52-1*341441-
Beta-Ala-R11050052280000

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References


View all 17 references: Citation Explorer
Direct detection of cysteine peptidases for MALDI-TOF MS analysis using fluorogenic substrates.
Authors: Elpidina, Elena N and Semashko, Tatiana A and Smirnova, Yulia A and Dvoryakova, Elena A and Dunaevsky, Yakov E and Belozersky, Mikhail A and Serebryakova, Marina V and Klyachko, Elena V and Abd El-Latif, Ashraf O and Oppert, Brenda and Filippova, Irina Y
Journal: Analytical biochemistry (2019): 45-50
Catalytic Mechanism of Cruzain from Trypanosoma cruzi As Determined from Solvent Kinetic Isotope Effects of Steady-State and Pre-Steady-State Kinetics.
Authors: Zhai, Xiang and Meek, Thomas D
Journal: Biochemistry (2018): 3176-3190
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
Recombinant expression and biochemical characterisation of two alanyl aminopeptidases of Trypanosoma congolense.
Authors: Pillay, Davita and Boulangé, Alain F V and Coustou, Virginie and Baltz, Théo and Coetzer, Theresa H T
Journal: Experimental parasitology (2013): 675-84
A quantitative technique for determining proteases and their substrate specificities and pH optima in crude enzyme extracts.
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Journal: Analytical biochemistry (2009): 56-62
Cold-induced apoptosis of rat liver endothelial cells: involvement of the proteasome.
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Journal: Transplantation (2003): 1946-53
Comparison of different peptidase substrates for evaluation of microbial quality of aerobically stored meats.
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Journal: Journal of food protection (2000): 1447-9
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Journal: Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan (2000): 909-21
Potent homophthalimide-type inhibitors of B16F10/L5 mouse melanoma cell invasion.
Authors: Kagechika, H and Komoda, M and Fujimoto, Y and Koiso, Y and Takayama, H and Kadoya, S and Miyata, K and Kato, F and Kato, M and Hashimoto, Y
Journal: Biological & pharmaceutical bulletin (1999): 1010-2
Cyclosporin A-cyclophilin complex formation. A model based on X-ray and NMR data.
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Journal: FEBS letters (1992): 291-300