Fluorogenic substrate for ECE-1 and ECE-2, ACE1 and ACE2, neprilysin, MMP-2 and MMP-9, thimet oligopeptidase, as well as cathepsin A, cathepsin X/Z, BACE, and insulinase, but not MMP-1.Mca fluorescence is quenched by the Dnp group until cleavage separates them. Ex.: 328nm, Em.: 393nm, although the following Ex/Em have also been used: 320-340/400-420. This substrate is useful for inhibitor screening and kinetic analysis.
Product Specification
| Sequence: | Mca-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys(Dnp)-OH[Mca=(7-methoxycoumarin-4-yl)acetyl;Dnp=2,4-dinitrophenyl] |
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| MW: | 1388.5 |
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| Source: | Synthetic. |
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| Formulation: | Lyophilized. |
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| Purity: | ≥98% (HPLC) |
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| Appearance: | White to off-white solid. |
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| Solubility: | Soluble in DMSO to at least 10mM. |
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| Shipping: | Shipped on Blue Ice |
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| Long Term Storage: | -20°C |
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| Use/Stability: | Store, as supplied, at -20°C for up to 1 year. Store solutions at -20°C for up to 3 months. |
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| Handling: | Protect from light and moisture. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Crystal structure of peptide-bound neprilysin reveals key binding interactions: S. Moss, et al.; FEBS Lett. (2019),
Abstract;
Beneficial Effects of Combined AT1 Receptor/Neprilysin Inhibition (ARNI) Versus AT1 Receptor Blockade Alone in the Diabetic Eye: T. Prasad, et al.; Invest. Ophthalmol. Vis. Sci.
57, 6722 (2016),
Abstract;
Full Text
Phosphinic tripeptides as dual angiotensin-converting enzyme C-domain and endothelin-converting enzyme-1 inhibitors: N. Jullien, et al.; J. Med. Chem.
53, 208 (2010),
Abstract;
Flexibility in substrate recognition by thimet oligopeptidase as revealed by denaturation studies: J.A. Sigman, et al.; Biochem. J.
388, 255 (2005),
Abstract;
Full Text
Characterization of endothelin-converting enzyme-2. Implication for a role in the nonclassical processing of regulatory peptides: N. Mzhavia, et al.; J. Biol. Chem.
278, 14704 (2003),
Abstract;
Full Text
Development of an internally quenched fluorescent substrate selective for endothelin-converting enzyme-1: G.D. Johnson & K. Ahn; Anal. Biochem.
286, 112 (2000),
Abstract;
