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Matrix metalloproteinase-19 (MMP-19) fluorometric drug discovery kit, RED



BML-AK307-0001	96 wells	693.00 USD
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The MMP-19 Fluorometric (also known as fluorimetric) Drug Discovery Kit, RED is a complete assay system designed to screen MMP-19 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-19, a potential therapeutic target. The compound NNGH is also included as a prototypic control inhibitor.

Product Details

Alternative Name:	RASI

Applications:	Fluorescent detection, HTS Activity assay

Application Notes:	Designed to screen MMP-19 inhibitors using a quenched fluorogenic peptide.

Handling:	Avoid freeze/thaw cycles.

Shipping:	Dry Ice

Long Term Storage:	-80°C

Contents:	1 vial MMP-19 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-19 (MMP-19, RASI; was initially named MMP-181) 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-19 include aggrecan, fibronectin, type I gelatin, and basement membrane components such as laminin, nidogen, and type IV collagen. MMP-19 is an important target for inhibitor screening due to its involvement in diseases such as angiogenesis, cancer, rheumatoid arthritis, multiple sclerosis, and psoriasis.

Technical Info/Product Notes:	NCBI Reference Sequence: NM_002429 The OMNIMMP^® RED substrate offers key advantages over other MMP substrates. 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. MMP substrate peptides display poor aqueous solubility, often with K_ms near their limits of solubility, making enzyme and inhibitor kinetics difficult. MMP K_ms for OMNIMMP^® RED substrate are below its solubility limit. In addition to the efficient binding as exhibited by low K_ms, OMNIMMP^® RED is avidly cleaved by MMPs, with k_cat/K_ms in the range of 10⁴-10⁶ M^-1sec^-1. The ultra-strong fluorescence of OMNIMMP^® RED allows for substrate concentrations much lower than the K_m, a condition generally desirable in inhibitor screening assays.

UniProt ID:	Q99542

Regulatory Status:	RUO - Research Use Only

General Literature References

Matrix metalloproteinases: regulators of the tumor microenvironment: K. Kessenbrock & Z. Werb; Cell 141, 52 (2010), Abstract;

MMP19 is upregulated during melanoma progression and increases invasion of melanoma cells: M. Muller, et al.; Mod. Pathol. 23, 511 (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;

VEGF and angiogenesis in acute and chronic MOG((35-55)) peptide induced EAE: W.A. Roscoe, et al.; J. Neuroimmunol. 209, 6 (2009), Abstract;

Matrix metalloproteinase 19 is highly expressed in active multiple sclerosis lesions: J. van Horssen, et al.; Neuropathol. Appl. Neurobiol. 32, 585 (2006), Abstract;

Matrix metalloproteinase-19 is expressed by keratinocytes in psoriasis: J. van Horssen, et al.; Acta Derm. Venereol. 83, 108 (2003),

Matrix metalloproteinases: they're not just for matrix anymore!: L.J. McCawley & L.M. Matrisian; Curr. Opin. Cell Biol. 13, 534 (2001), Abstract;

Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme: J.O. Stracke, et al.; J. Biol. Chem. 275, 14809 (2000), Abstract;

Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP): J.O. Stracke, et al.; FEBS Lett. 478, 52 (2000), 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;

Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution: A.M. Pendas, et al.; J. Biol. Chem. 272, 4281 (1997), Abstract;

The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels of a rheumatoid arthritis patient: C. Kolb, et al.; Immunol. Lett. 57, 83 (1997), Abstract;

Identification of MMP-18, a putative novel human matrix metalloproteinase: J. Cossins, et al.; Biochem. Biophys. Res. Commun. 228, 494 (1996), Abstract;