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MMP substrate α (fluorogenic)

BML-P131

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Fluorogenic substrate for several matrix metalloproteinases (MMPs). It is cleaved by MMP-1 (k_cat/K_m=3.3x10M^-1s^-1), MMP-2 (k_cat/K_m=5.8×10), MMP-3 (k_cat/K_m=2.2×10), MMP-7 (k_cat/K_m=1.2×10), MMP-8, MMP-9 (k_cat/K_m=6.9×10), and MMP-26 (k_cat/K_m=4.9×10) 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.

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Product Details

Alternative Name	Matrix metalloproteinase substrate α
CAS	121282-17-5
Formula	C₄₅H₆₄N₁₄O₁₁
MW	977.09
Purity	≥94% (HPLC)
Sequence	Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH₂ (Dnp=2,4-dinitrophenyl)

Handling & Storage

Use/Stability	As indicated on product label or CoA when stored as recommended.
Long Term Storage	-20°C
Shipping	Blue Ice

Regulatory Status	RUO – Research Use Only

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

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MMP substrate α (fluorogenic)

BML-P131

Product Details

Handling & Storage

Datasheet, Manuals, SDS & CofA

Manuals And Inserts

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