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MMP substrate α (fluorogenic)

BML-P131-0001 1 mg 147.00 USD
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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
Sequence:Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 (Dnp=2,4-dinitrophenyl)
Purity:≥94% (HPLC)
Shipping:Blue Ice
Long Term Storage:-20°C
Regulatory Status:RUO - Research Use Only

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; Full Text