A QUANTIZYME® Assay System. The MMP-9 Fluorometric (also known as fluorimetric) Drug Discovery Kit is a complete assay system designed to screen inhibitors of matrix metalloproteinase-9 (MMP-9, gelatinase B) using a quenched fluorogenic peptide: OMNIMMP® fluorogenic substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH. Mca fluorescence is quenched by the Dpa group until cleavage by MMPs at the Gly-Leu bond 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. Included are active enzyme, assay buffer, a prototypic control inhibitor (NNGH)3, and a detailed instruction booklet.
Elevated Neutrophil Elastase in Tears of Ocular Graft-Versus-Host Disease Patients: S.N. Arafat, et al.; Am. J. Ophthalmol. 176, 46 (2017), Abstract;
Tear Matrix Metalloproteinases and Myeloperoxidase Levels in Patients With Boston Keratoprosthesis Type I: M.C. Robert, et al.; Cornea 35, 1008 (2016), Abstract; Full Text
Neutrophil collagenase, gelatinase, and myeloperoxidase in tears of patients with stevens-johnson syndrome and ocular cicatricial pemphigoid: S.N. Arafat, et al.; Ophthalmology 121, 79 (2014), Abstract; Full Text
Targeting androgen receptor/Src complex impairs the aggressive phenotype of human fibrosarcoma cells: G. Castoria, et al.; PLoS One 8, e76899 (2013), Abstract; Full Text
Interplay between steroid receptors and neoplastic progression in sarcoma tumors: A. Fiorelli, et al.; J. Cell. Physiol. 226, 2997 (2011), Abstract;
Negative regulation of stress-induced matrix metalloproteinase-9 by Sirt1 in skin tissue: J.S. Lee, et al.; Exp. Dermatol. 19, 1060 (2010), Abstract;
Produced in E. coli. Active recombinant matrix metalloproteinase-9 (MMP-9, gelatinase B, 92 kDa type IV collagenase) cloned from human cDNA. The enzyme consists of residues Phe107-Pro449 (NM_004994), which comprises the catalytic/fibronectin domain of human MMP-9, with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-9 which lacks the C-terminal hemopexin domain. Activity toward its targets, such as gelatin, casein, or peptide substrates, is unaffected., ≥95% (SDS-PAGE) | Print as PDF