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MMP substrate (fluorogenic)

BML-P128-0001 1 mg 250.00 USD
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Fluorogenic substrate for several matrix metalloproteinases (MMPs). It is cleaved by MMP-1, MMP-3, MMP-7, MMP-8, MMP-9, MMP-11, MMP-12, MMP-13, and ADAM9/MDC9, but only slightly by MMP-2 and not at all by ADAM17/TACE. Ex/Em= 340nm/440nm, although 365/450 is also appropriate. Highly quenched, with strong fluorescence by Nma at 440nm once cleavage separates it from the aromatic Dnp moiety. Compatible with most fluorometers.

Product Details

Alternative Name:Matrix metalloproteinase substrate, Dnp-Pro-β-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(Nma)-NH2
Purity:≥98% (HPLC)
Appearance:lyophylized solid
Solubility:Soluble in DMSO (at least 20mM).
Shipping:Blue Ice
Long Term Storage:-20°C
Handling:Protect from light.
Regulatory Status:RUO - Research Use Only

Product Literature References

Chemical Composition and Effect against Skin Alterations of Bioactive Extracts Obtained by the Hydrodistillation of Eucalyptus globulus Leaves: P. Moreira, et al.; Pharmaceutics 14, 561 (2022), Abstract;
Parenchymal border macrophages regulate the flow dynamics of the cerebrospinal fluid: A. Drieu, et al.; Nature 611, 585 (2022), Abstract;
Polyphenol-Rich Extracts Obtained from Winemaking Waste Streams as Natural Ingredients with Cosmeceutical Potential: M.S. Matos, et al.; Antioxidants 8, 355 (2019), Application(s): Substrate in MMP-1 activity assays., Abstract; Full Text
Targeting mechanotransduction mechanisms and tissue weakening signals in the human amniotic membrane: D.W. Barrett, et al.; Sci. Rep. 9, 6718 (2019), Abstract; Full Text
Nucleic acid-induced potentiation of matrix metalloproteinase-9 enzymatic activity: T. Duellman, et al.; Biochem. J. 475, 1597 (2018), Abstract; Full Text
Toll-Like Receptor 4-Independent Carbon Tetrachloride-Induced Fibrosis and Lipopolysaccharide-Induced Acute Liver Injury in Mice: Role of Hepatic Stellate Cells: S. Kumar, et al.; Am. J. Pathol. 187, 1356 (2017), Abstract; Full Text
The tumor necrosis factor-alpha converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity: M.J. Mohan, et al.; Biochemistry 41, 9462 (2002), Abstract;
N-Aryl sulfonyl homocysteine hydroxamate inhibitors of matrix metalloproteinases: further probing of the S(1), S(1)’, and S(2)’ pockets: S. Hanessian, et al.; J. Med. Chem. 44, 3066 (2001), Abstract;
Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity: M. Roghani, et al.; J. Biol. Chem. 274, 3531 (1999), Abstract;
Detection system for reaction-rate analysis in a low-volume proteinase-inhibition assay: W.P. Ambrose, et al.; Anal. Biochem. 263, 150 (1998), Abstract;
Evaluation of fluorometric and zymographic methods as activity assays for stromelysins and gelatinases.: A.R. Quesada, et al.; Clin. Exp. Metastasis 15, 26 (1997), Abstract;
A high throughput fluorogenic substrate for interstitial collagenase (MMP-1) and gelatinase (MMP-9): D.M. Bicket, et al.; Anal. Biochem. 212, 58 (1993), Abstract;

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