| CAS | 140430-53-1 |
| Sequence | Mca-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 |
| Sequence Single | Mca-PLGL-Dpa-AR-NH2 |
| Molecular Formula | C49H68N14O15 |
| Molecular Weight | 1093.16 |
| Synonyms | 7-Methoxycoumarin-4-Acetyl-Pro-Leu-Gly-Leu-Dnp-(2,3-Diaminopropionyl)-Ala-Arg, amide |
| Technology | Synthetic |
| Storage | -20°C, avoid light, cool and dry place |
| Application | Cancer Research |
| Description | Mca-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 is a very sensitive FRET substrate for continuous assays and in situ determination of the matrix metalloproteinase(MMP-2) and MMP-7 activity with positive charge. Cleavage at the Gly-Leu bond separates the highly fluorescent Mca group from the efficient 2,4-dinitrophenyl quencher, resulting in an increase in fluorescence intensity. The kcat/Km values for the punctuated metalloproteinase (MMP-7) and for gelatinase (MMP-2), e.g., are 1.7·10⁵ and 6.3·10⁵ M-1s-1, respectively. |
| References | 1. Comparative properties of recombinant human and bovine matrix metalloproteinase-20. R.Drozdz et al., Peptides 1994, Proceedings of the 23rd European Peptide Symposium, Braga, p. 785, H.L.S.Maia, ed., Escom, Leiden, (1995) 2. Substrate-dependent activation of thermolysin by salt. L.Zhu et al., Arch. Oral Biol., 53, 785 (2008) 3. 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. H.Oneda et al., Biosci. Biotechnol. Biochem., 68, 1811 (2004) 4. Development of new hydroxamate matrix metalloproteinase inhibitors derived from functionalized 4-aminoprolines. U.Neumann et al., Anal. Biochem., 328, 166 (2004) 5. Microscopic localization of active proteases by in situ zymography: detection of matrix metalloproteinase activity in vascular tissue. M.G.Natchus et al., J. Med. Chem., 43, 4948 (2000) |