Mu hssklq amc

Manufactured by Merck Group

Sourced in Switzerland

Mu-HSSKLQ-AMC is a fluorogenic substrate used for the detection and quantification of protease activity. It consists of a peptide sequence (Mu-HSSKLQ) linked to a fluorescent molecule (AMC). When the peptide is cleaved by a target protease, the release of the fluorescent AMC moiety can be measured, providing a direct readout of the protease's activity.

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Lab products found in correlation

Z rlrgg amc, by Bachem (1 mentions)

2 protocols using mu hssklq amc

Fluorogenic Enzyme Assay for PSA

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PSA (pure grade >96%), obtained from seminal fluid, was purchased by SunnyLab (SCIPAC Ltd, Sittingbourne, UK). The highly-specific PSA fluorogenic substrate Mu-HSSKLQ-AMC (purity >97%) was purchased from Sigma-Aldrich (Buchs, Switzerland).
The PSA-catalyzed hydrolysis of Mu-HSSKLQ-AMC was monitored spectrofluorimetrically at 460 nm with a Cary Eclipe spectrofluorimeter (Varian, Palo Alto, Ca, USA). The excitation wavelength was 380 nm with a slit bandwidth of 5 nm. The Mu-HSSKLQ-AMC concentration ranged between 5 and 70 µM, whereas the PSA concentration was 50 nM for all determinations. The PSA-catalyzed hydrolysis of Mu-HSSKLQ-AMC was investigated between pH 6.5 and 9.0 using the following buffers: 25 mM bis-tris-HCl and 25 mM tris-HCl, in the presence of 100 mM NaCl, 10 mM CaCl₂, and 0.05% Brij (a nonionic detergent). All measurements were performed at 37.0°C.

Tomao L., Sbardella D., Gioia M., Di Masi A., Marini S., Ascenzi P, & Coletta M. (2014). Characterization of the Prostate-Specific Antigen (PSA) Catalytic Mechanism: A Pre-Steady-State and Steady-State Study. PLoS ONE, 9(7), e102470.

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SARS-CoV-2 3CLpro and PL Inhibition Assays

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Recombinant SARS-CoV-2 3CLpro (100 nM) was assayed at 25°C in either (a) in 30 μL reaction volumes containing 20 mM Tris-HCl pH 7.5, 150 mM NaCl, 1 mM DTT, 5 % glycerol, 0.01% Tween 20 100 μM of Mu-HSSKLQ-AMC (Sigma-Aldrich, SCP0224), in 384-well black plates in triplicate or (b) in 50 μL reaction mixtures containing 20 mM Tris-HCl pH 7.5, 150 mM NaCl, 0.1 mM EDTA, 2 mM DTT, 10% DMSO, and 25–50 nM 3CLpro in 96-well plates (Greiner, flat-bottom half volume, clear black plates), using the FRET-based substrate Abz-SAVLQSGFRK(DNP)-NH₂ wherein peptidolysis was measured at 320/420 nm (ex/em) (Biotek® Synergy M2) in the presence and absence of 0–50 μM K777 in duplicate. Recombinant SARS-CoV-2 PL was assayed in either (a) 50 mM HEPES, 150 mM NaCl, 1 mM DTT, 0.01% Tween 20; pH 6.5 buffer using 50 μM Z-RLRGG-AMC (Bachem, I1690) and 24.5 nM enzyme or (b) 50 mM HEPES pH 7.5, 5 mM DTT, 0.1 mg/mL BSA, 2% DMSO, 50 μM Z-RLRGG-AMC, and 10 nM PL, where rates in the presence and absence of K777 were measured at 360/460 nm (ex/em). In some studies, enzymes were pre-incubated with 20 μM of K777 or 0.0025 % DMSO for 15 minutes and then diluted in an equal volume of substrate in assay buffer.

Mellott D.M., Tseng C.T., Drelich A., Fajtová P., Chenna B.C., Kostomiris D.H., Hsu J., Zhu J., Taylor Z.W., Tat V., Katzfuss A., Li L., Giardini M.A., Skinner D., Hirata K., Beck S., Carlin A.F., Clark A.E., Beretta L., Maneval D., Frueh F., Hurst B.L., Wang H., Kocurek K.I., Raushel F.M., O’Donoghue A.J., de Siqueira-Neto J.L., Meek T.D, & McKerrow J.H. (2020). A cysteine protease inhibitor blocks SARS-CoV-2 infection of human and monkey cells. bioRxiv.

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