Sensitive fluorogenic substrate for most matrix metalloproteinase (MMP) enzymes, as follows [kcat/Km (M-1s-1) and Km (µM), in parentheses]: MMP-1 (9.2 x 104, 27); MMP-2 (6.9x105, >30); MMP-3 (2.0x104); MMP-7 (2.9x105); MMP-8 (4.2x105); MMP-9 (6.2x105, >30); MMP-12 (1.3x105, 130); MMP-13 (1.1x106, 5.2); MMP-14 (1.3x106, 7.9); mouse, rat, and monkey MMP-14; MMP-16; MMP-20; ADAM10 (1.1x103); ADAM17/TACE (7.8x105, 26), and BACE2 (internal data using Prod. No. BML-SE550). It is cleaved very poorly by neutrophil elastase, and not at all by trypsin. Can be used to measure cell-associated activity, or activity in cell-conditioned medium, or in biological fluids such as synovial fluid. Mca fluorescence is quenched by the Dpa group until cleavage separates them (MMPs cleave between Gly-Leu). Ex.: 328nm, Em.: 400nm, but it is possible to use Ex./Em. 320-340/393-420nm. This highly-quenched (98.4%) substrate is useful for inhibitor screening and kinetic analysis.
Product Details
| Alternative Name: | FS-6 |
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| Sequence: | Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2·TFA [Mca=(7-methoxycoumarin-4-yl)acetyl; Dpa=N-3-(2,4-dinitrophenyl)-L-α,β-diaminopropionyl] |
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| Formula: | C55H80N16O16 . CF3CO2H |
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| MW: | 1221.3 . 114.0 |
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| CAS: | 720710-69-0 |
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| Purity: | ≥98% (HPLC) |
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| Appearance: | Lyophilized yellow solid. |
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| Solubility: | Soluble in water (10mg/ml). |
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| Shipping: | Blue Ice |
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| Long Term Storage: | -20°C |
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| Handling: | Protect from light. |
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| Technical Info/Product Notes: | Also available: OMNIMMP® fluorogenic control peptide Mca-Pro-Leu-OH (Prod. No. BML-P127). |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Chemical Optimization of Selective Pseudomonas aeruginosa LasB Elastase Inhibitors and Their Impact on LasB-Mediated Activation of IL-1β in Cellular and Animal Infection Models: M.J. Everett, et al.; ACS Infect. Dis.
9, 270 (2023),
Abstract;
High-throughput proteomics and in vitro functional characterization of the 26 medically most important elapids and vipers from sub-Saharan Africa: G.T.T. Nguyen, et al.; Gigascience
11, giac121 (2022),
Abstract;
Identification of a Common Pharmacophore for Binding to MMP2 and RGD Integrin: Towards a Multitarget Approach to Inhibit Cancer Angiogenesis and Metastasis: L. Baldini, et al.; Molecules
27, 1249 (2022),
Abstract;
Biphenyl substituted lysine derivatives as recognition elements for the matrix metalloproteinases MMP-2 and MMP-9: A. Kirchhain, et al.; Bioorg. Chem.
115, 105155 (2021),
Abstract;
Neuroprotective Effects of Methyl Caffeate against Hydrogen Peroxide-Induced Cell Damage: Involvement of Caspase 3 and Cathepsin D Inhibition: D. Jantas, et al.; Biomolecules
10, 1530 (2020),
Abstract;
Full Text
SARS-CoV-2 spike protein promotes IL-6 trans-signaling by activation of angiotensin II receptor signaling in epithelial cells: T. Patra, et al.; PLoS Pathog.
16, e1009128 (2020),
Abstract;
Full Text
A pilot study of active enzyme levels in gingival crevicular fluid of patients with chronic periodontal disease: S.S. Gul, et al.; J. Clin. Periodontol.
43, 629 (2016),
Application(s): MMP activity in gingival crevicular fluid (GCF),
Abstract;
Defining a new diagnostic assessment parameter for wound care: Elevated protease activity, an indicator of nonhealing, for targeted protease‐modulating treatment: T.E. Serena, et al.; Wound Repair Regen.
24, 589 (2016),
Application(s): MMP activity in chronic wound swab samples,
Abstract;
Improved clinical outcome and biomarkers in adults with papulopustular rosacea treated with doxycycline modified-release capsules in a randomized trial: A. Di Nardo, et al.; J. Am. Acad. Dermatol.
74, 1086 (2016),
Application(s): Measurement of protease activity from skin surface tape stripping's,
Abstract;
Disposable MMP-9 sensor based on the degradation of peptide cross-linked Hydrogel films using electrochemical impedance spectroscopy: A. Biela, et al.; Biosens. Bioelectron.
68C, 660 (2015),
Abstract;
Mast cells are key mediators of cathelicidin-initiated skin inflammation in rosacea: Y. Muto, et al.; J. Invest. Dermatol.
134, 2728 (2014),
Application(s): MMP activity in cell lysates,
Abstract;
Full Text
General Literature References
Inflammatory mediators and cartilage biomarkers in synovial fluid after a single inflammatory insult: a longitudinal experimental study: J.C. de Grauw, et al.; Arthritis. Res. Ther.
11, R35 (2009),
Abstract;
Selective inhibition of matrix metalloproteinase-14 blocks tumor growth, invasion, and angiogenesis: L. Devy, et al.; Cancer Res.
69, 1517 (2009),
Abstract;
Dual inhibitors of matrix metalloproteinases and carbonic anhydrases: iminodiacetyl-based hydroxamate-benzenesulfonamide conjugates: S.M. Marques, et al.; J. Med. Chem.
51, 7968 (2008),
Abstract;
Reduced amelogenin-MMP20 interactions in amelogenesis imperfecta: K. Tanimoto, et al.; J. Dent. Res.
87, 451 (2008),
Abstract;
Rapid determination of enzyme kinetics from fluorescence: overcoming the inner filter effect: M.O. Palmier & S.R. Van Doren; Anal. Biochem.
371, 43 (2007),
Abstract;
Characterization of Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2, a fluorogenic substrate with increased specificity constants for collagenases and tumor necrosis factor converting enzyme: U. Neumann, et al.; Anal. Biochem.
328, 166 (2004),
Abstract;
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