Fluorogenic substrate for several matrix metalloproteinases (MMPs). It is cleaved by MMP-1 (kcat/Km=3.3x10M-1s-1), MMP-2 (kcat/Km=5.8x10), MMP-3 (kcat/Km=2.2x10), MMP-7 (kcat/Km=1.2x10), MMP-8, MMP-9 (kcat/Km=6.9x10), and MMP-26 (kcat/Km=4.9x10) Ex/Em=280nm/346nm, although 283/350,360 are also appropriate. Fluorescence at 346 nm by tryptophan occurs once cleavage separates it from the quenching aromatic Dnp moiety. MMPs cleave this peptide between Gly-Leu.
Product Details
| Alternative Name: | Matrix metalloproteinase substrate α |
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| Sequence: | Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 (Dnp=2,4-dinitrophenyl) |
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| Formula: | C45H64N14O11 |
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| MW: | 977.09 |
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| CAS: | 121282-17-5 |
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| Purity: | ≥94% (HPLC) |
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| Shipping: | Blue Ice |
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| Long Term Storage: | -20°C |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Biochemical characterization and zinc binding group (ZBGs) inhibition studies on the catalytic domain of MMP7 (cdMMP7): F. Meng, et al.; J. Inorg. Biochem.
1656, 7 (2016),
Abstract;
7-Ketocholesterol and cholesterol-5α,6α-epoxide induce smooth muscle cell migration and proliferation through the epidermal growth factor receptor/phosphoinositide 3-kinase/Akt signaling pathways: P. L. Liao, et al.; Toxicol. Lett.
197, 88 (2010),
Application(s): Measurement of MMP activity in 7-keto- or α-epoxide-treated and untreated, concentrated smooth muscle cell media,
Abstract;
Activation of PPARs α, β/δ, and γ Impairs TGF-β1-Induced Collagens' Production and Modulates the TIMP-1/MMPs Balance in Three-Dimensional Cultured Chondrocytes: P.E. Poleni, et al.; PPAR Res.
2010, 635912 (2010),
Application(s): Measurement of global MMP activities in culture supernatants of rat primary chondrocytes,
Abstract;
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