Mca-YVADAPK(Dnp)-OH Fluorogenic Peptide Substrate
R&D Systems | Catalog # ES007
Key Product Details
Conjugate
Applications
Product Specifications
Source
Mca-Tyr-Val-Ala-Asp-Ala-Pro-Lys(Dnp)-OH.
Mca: (7-Methoxycoumarin-4-yl)acetyl, Dnp: 2, 4-Dinitrophenyl.
Purity
Predicted Molecular Mass
Activity
It is an excellent substrate for caspase-1/interleukin-converting enzyme (ICE) and angiotensin I-converting enzyme-2 (ACE-2) (Enari, M. et al., 1996, Nature 380:723; Vickers, C. et al., 2002, J. Biol. Chem. 277:14838). The cleavage sites by ICE and ACE-2 are the peptide bonds between Ala and Asp and between Pro and Lys, respectively.
Reviewed Applications
Read 2 reviews rated 5 using ES007 in the following applications:
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ES007
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Samples are stable for up to twelve months from date of receipt at -20° C to -70° C. The substrate can be aliquoted and stored -20° C to -70° C in a manual defrost freezer for six months. Avoid repeated freeze-thaw cycles. Protect from exposure to direct light. |
Product Documents for Mca-YVADAPK(Dnp)-OH Fluorogenic Peptide Substrate
Certificate of Analysis
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Product Specific Notices for Mca-YVADAPK(Dnp)-OH Fluorogenic Peptide Substrate
For research use only
Citations for Mca-YVADAPK(Dnp)-OH Fluorogenic Peptide Substrate
Customer Reviews for Mca-YVADAPK(Dnp)-OH Fluorogenic Peptide Substrate (2)
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Application: Enzymatic activity in vitroVerified Customer | Posted 12/04/2020
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Verified Customer | Posted 08/04/2016ACE-2 activity was determined following incubation with intramolecularly quenched synthetic ACE-2 specific substrate 7-Mca-YVADAPK (Dnp) (R&D systems). In the case of cell lysates, 10 µg of total protein was assayed for activity in a buffer with the following composition: 50 mM MES (4-morpholineethanesulphonic acid), 300 mM NaCl, 10 µm ZnCl2 and 0.01% Triton X-100, pH 6.5. Reaction was initiated by the addition of 5×10−5 M substrate. Where applicable, recombinant enzymes were used at a concentration of 0.01 µg per reaction. The fluorescence measurements were performed in the black microtiter plates (Costar) in a total volume of 100 µl. The plates were read using a fluorescence plate reader SpectraMax M5 (Molecular Devices) at an excitation wavelength 320 nm and emission wavelength 405 nm Fluorescence resulting from the substrate hydrolysis increased with time, and achieved maximum by one h with recombinant enzyme.
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