Matrix metalloproteinase-9 (MMP-9) fluorometric drug discovery kit, RED



BML-AK306-0001	96 wells	714.00 USD
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The MMP-9 Fluorometric (also known as fluorimetric) Drug Discovery Kit, RED is a complete assay system designed to screen MMP-9 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-9, a potential therapeutic target. The compound NNGH is also included as a prototypic control inhibitor.

Product Details

Alternative Name:	Gelatinase B, 92kDa Type IV collagenase

Applications:	Fluorescent detection, HTS Activity assay

Handling:	Avoid freeze/thaw cycles.

Shipping:	Dry Ice

Long Term Storage:	-80°C

Contents:	1 vial MMP-9 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-9 (MMP-9, gelatinase B, 92kDa type IV collagenase) 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-9 include native and denatured collagens, fibronectin, elastin, laminin, pro-TNF-α, and interleukins and their receptors. MMP-9 is secreted as a 92kDa proenzyme (as measured by SDS-PAGE), and activated by cleavage to forms 82kDa and smaller. MMP-9 is an important target for inhibitor screening due to its involvement in diseases such as alopecia, cancer, angiogenesis, and metastasis.

Technical Info/Product Notes:	NCBI Reference Sequence: NM_004994 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 well below its solubility limit. OMNIMMP^® RED is avidly cleaved by MMPs, with k_cat/K_ms in the range of ~10⁴-10⁶M^-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:	P14780

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;

Updated biological roles for matrix metalloproteinases and new "intracellular" substrates revealed by degradomics : G.S. Butler & C.M. Overall; Biochemistry 48, 10830 (2009), Abstract;

A novel role of metalloproteinase in cancer-mediated immunosupression: B.-C. Sheu, et al.; Cancer Res. 61, 237 (2001), Abstract; Full Text

Identification of clustered cells in the human hair follicle responsible for MMP-9 gelatinolytic activity: consequences for the regulation of hair growth: F. Jarrousse, et al.; Int. J. Dermatol. 40, 385 (2001), Abstract;

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

Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis: G. Bergers, et al.; Nat. Cell Biol. 2, 737 (2000), Abstract; Full Text

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;

Analysis of the role of the COOH-terminal domain in the activation, proteolytic activity, and tissue inhibitor of metalloproteinase interactions of gelatinase B: J.P. O'Connell, et al.; J. Biol. Chem. 269, 14967 (1994), Abstract;