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Matrix metalloproteinase-3 (MMP-3) fluorometric drug discovery kit, RED

 
BML-AK311-0001 96 wells 525.00 USD
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The MMP-3 Fluorometric (also known as fluorimetric) Drug Discovery Kit, RED is a complete assay system designed to screen MMP-3 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-3, a potential therapeutic target. The compound NNGH is also included as a prototypic control inhibitor.

Product Specification

Alternative Name:Stromelysin-1, Transin-1
 
Applications:Fluorescent detection, HTS
Activity assay
 
Application Notes:Designed to screen MMP-3 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-3 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-3 (MMP-3, stromelysin-1, transin-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-3 include collagens, fibronectin, and laminin, plasminogen, HB-EGF, E-cadherin, and other MMPs. MMP-3 is secreted as a 55-59kDa glycosylated proenzyme (measured by SDS-PAGE), and activated by cleavage to forms of 21-48kDa.  It is unique from other MMPs in that its pH optimum is 5.9, rather than around 7.0.
 
Technical Info/Product Notes:NCBI Reference Sequence: NM_002422

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. 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:P08254
 

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),
Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1.: V. Noë et al.; J. Cell Sci. 114, 111 (2001),
A rationalization of the acidic pH dependence for stromelysin-1 (matrix metalloproteinase-3) catalysis and inhibition: L.L. Johnson, et al.; J. Biol. Chem. 275, 11026 (2000), Abstract; Full Text
Matrix metalloproteinase degradation of extracellular matrix: biological consequences.: S.D. Shapiro; Curr. Opin. Cell Biol. 10, 602 (1998),
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;

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