Matrix metalloproteinase-1 (MMP-1) fluorometric drug discovery kit, RED



BML-AK301-0001	96 wells	714.00 USD
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The MMP-1 Fluorometric (also known as fluorimetric) Drug Discovery Kit, RED is a complete assay system designed to screen MMP-1 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-1, a potential therapeutic target. The compound NNGH is also included as a prototypic control inhibitor.

Product Details

Alternative Name:	Interstitial collagenase, Fibroblast collagenase

Applications:	Fluorescent detection, HTS Activity assay

Application Notes:	Designed to screen MMP-1 inhibitors using a quenched fluorogenic peptide

Handling:	Avoid freeze/thaw cycles.

Shipping:	Dry Ice

Long Term Storage:	-80°C

Contents:	1 vial MMP-1 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-1 (MMP-1, interstitial collagenase, fibroblast 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-1 include collagen, gelatin, entactin, pro-TNF-α, and the chemokine SDF-1. MMP-1 is secreted as a 52-56kDa glycosylated proenzyme (as measured by SDS-PAGE), and activated by cleavage to forms of 22-46kDa. MMP-1 is an important target for inhibitor screening due to its involvement in diseases such as cancer.

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. 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:	P03956

Regulatory Status:	RUO - Research Use Only

Product Literature References

Acetylated Resveratrol and Oxyresveratrol Suppress UVB-Induced MMP-1 Expression in Human Dermal Fibroblasts: J.E. Lee, et al.; Antioxidants 10, 1252 (2021), Abstract;

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;

Identification of MMP-1 as a putative breast cancer predictive marker by global gene expression analysis: I. Poola et al.; Nat. Med. 11, 481 (2005), Abstract;

Matrix Metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1: G.A. McQuibban; J. Biol. Chem. 276, 43503 (2001), Abstract;

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

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;

Mechanisms of activation of tissue procollagenase by matric metalloproteinase 3 (stromelysin): K. Suzuki, et al.; Biochemistry 29, 10261 (1990), Abstract;