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Matrix metalloproteinase-7 (MMP-7) fluorometric drug discovery kit, RED

 
BML-AK304-0001 96 wells 424.00 GBP
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The MMP-7 Fluorometric (also known as fluorimetric) Drug Discovery Kit, RED is a complete assay system designed to screen MMP-7 inhibitors using a quenched fluorogenic substrate OMNIMMP® RED: TQ3-GABA-Pro-Cha-Abu-Smc-His-Ala-Dab(6-TAMRA)-Ala-Lys-NH2 [TQ3=quencher; GABA=4-aminobutyric acid; Cha=L-cyclohexylalanine; Abu=2-aminobutyric acid; Smc=S-methyl-L-cysteine; Dab=2,4-diaminobutyric acid; 6-TAMRA=6-tetramethylrhodamine]. TAMRA fluorescence is thoroughly quenched by the TQ3 group until cleavage by MMPs separates the two moieties.

The assays are performed in a convenient 96-well microplate format. The kit is useful to screen inhibitors of MMP-7, a potential therapeutic target. The compound NNGH is also included as a prototypic control inhibitor.

Product Specification

Alternative Name:Matrilysin, Pump
 
Applications:Fluorescent detection, HTS
Activity assay
 
Application Notes:Designed to screen MMP-7 inhibitors using a quenched fluorogenic peptide.
 
Handling:Avoid freeze/thaw cycles.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Kit/Set Contains:1 vial MMP-7 enzyme
1 vial substrate (OMNIMMP® RED)
1 vial 6'-TAMRA calibration standard
1 vial control inhibitor (NNGH)
1 bottle (20 ml) assay buffer
1 black 96-well microplate
Instructions
 
Scientific Background:Matrix metalloproteinase-7 (MMP-7, matrilysin, pump-1) is a member of the MMP family of extracellular proteases.These enzymes play a role in many normal and disease states by virtue of their broad substrate specificities. Targets of MMP-7 include collagen, osteopontin, pro-TNF-α, E-cadherin, ß4 integrin, and Fas ligand. MMP-7 is secreted as a 28kDa proenzyme (as measured by SDS-PAGE), and activated by cleavage to 19kDa. MMP-7 is an important target for inhibitor screening due to its involvement in diseases such as cancer.
 
Technical Info/Product Notes:NCBI Reference Sequence: NM_002423

The OMNIMMP® RED substrate offers key advantages over other MMP substrates.
  1. Emission at the red end of the spectrum (576 nm after excitation at 545 nm) avoids the interference at lower wavelengths often exhibited by screening compounds, and by substances commonly found in biological samples and tissue culture medium.
  2. MMP substrate peptides display poor aqueous solubility, often with Kms near their limits of solubility, making enzyme and inhibitor kinetics difficult.  MMP Kms for OMNIMMP® RED substrate are below its solubility limit.
  3. In addition to the efficient binding as exhibited by low Kms, OMNIMMP® RED is avidly cleaved by MMPs, with kcat/Kms in the range of 104-106 M-1sec-1.
  4. The ultra-strong fluorescence of OMNIMMP® RED allows for substrate concentrations much lower than the Km, a condition generally desirable in inhibitor screening assays.
 
UniProt ID:P09237
 

General Literature References

Matrix metalloproteinases: regulators of the tumor microenvironment: K. Kessenbrock & Z. Werb; Cell 141, 52 (2010), Abstract;
Updated biological roles for matrix metalloproteinases and new "intracellular" substrates revealed by degradomics : G.S. Butler & C.M. Overall; Biochemistry 48, 10830 (2009), Abstract;
Matrix metalloproteinases: they’re not just for matrix anymore!: L.J. McCawley & L.M. Matrisian; Curr. Opin. Cell Biol. 13, 534 (2001), Abstract;
Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin): R. Agnihotri, et al.; J. Biol. Chem. 276, 28261 (2001), Abstract; Full Text
The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis: W.C. Powell, et al.; Curr. Biol. 9, 1441 (1999), Abstract;
Discovery of CGS 27023A, a non-peptidic, potent, and orally active stromelysin inhibitor that blocks cartilage degradation in rabbits: L.J. MacPherson, et al.; J. Med. Chem. 40, 2525 (1997), Abstract;
Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloproteinases: T. Crabbe, et al.; Biochemistry 31, 8500 (1992), Abstract;

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