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Ac ala amc substrate

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The 20X Ac-Ala-AMC substrate is a fluorogenic peptide substrate used for the detection and measurement of enzymatic activity. It functions as a sensitive and specific substrate for various proteases, enabling the quantification of their catalytic activity through fluorescence-based assays.

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Lab products found in correlation

Clear bottom 96 well plate, by Corning (2 mentions)

2 protocols using ac ala amc substrate

1

Fluorometric Enzyme Inhibition Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
APEH (1 mg/mL) was diluted 1:20,000 in assay buffer (50 mM Tris, pH 7.5). 180 μL was added to each well on a 96-well clear bottom plate (Costar, Cat. No. 3603). 20 μL of inhibitor (diluted previously to 100x in assay buffer) was added to each sample and incubated for 10 min at 25 °C. 10 μL of 20X Ac-Ala-AMC substrate (Bachem, Cat. No. I-1830) in assay buffer was added and incubated for an additional 30 min at 25 °C, shaking the plate for the first two minutes. Fluorescence was read using 380 nm excitation and 460 nm emission wavelengths.
Bachovchin D.A., Koblan L.W., Wu W., Liu Y., Li Y., Zhao P., Woznica I., Shu Y., Lai J.H., Poplawski S.E., Kiritsy C.P., Healey S.E., DiMare M., Sanford D.G., Munford R.S., Bachovchin W.W, & Golub T.R. (2014). A high-throughput, multiplexed assay for superfamily-wide profiling of enzyme activity. Nature chemical biology, 10(8), 656-663.
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2

Fluorometric Enzyme Inhibition Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
APEH (1 mg/mL) was diluted 1:20,000 in assay buffer (50 mM Tris, pH 7.5). 180 μL was added to each well on a 96-well clear bottom plate (Costar, Cat. No. 3603). 20 μL of inhibitor (diluted previously to 100x in assay buffer) was added to each sample and incubated for 10 min at 25 °C. 10 μL of 20X Ac-Ala-AMC substrate (Bachem, Cat. No. I-1830) in assay buffer was added and incubated for an additional 30 min at 25 °C, shaking the plate for the first two minutes. Fluorescence was read using 380 nm excitation and 460 nm emission wavelengths.
Bachovchin D.A., Koblan L.W., Wu W., Liu Y., Li Y., Zhao P., Woznica I., Shu Y., Lai J.H., Poplawski S.E., Kiritsy C.P., Healey S.E., DiMare M., Sanford D.G., Munford R.S., Bachovchin W.W, & Golub T.R. (2014). A high-throughput, multiplexed assay for superfamily-wide profiling of enzyme activity. Nature chemical biology, 10(8), 656-663.
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