A QUANTIZYME® Assay System. The MMP-9 Colorimetric Drug Discovery Kit is a complete assay system designed to screen inhibitors of matrix metalloproteinase-9 (MMP-9, gelatinase B) using a thiopeptide as a chromogenic substrate. 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), and a detailed instruction booklet.
Toxicological effects of NCKU-21, a phenanthrene derivative, on cell growth and migration of A549 and CL1-5 human lung adenocarcinoma cells: H.F. Liao, et al.; PLoS One 12, e28945763 (2017), Abstract; Full Text
Novel in vitro inhibitory functions of potato tuber proteinaceous inhibitors: M. Fischer, et al.; Mol. Genet. Genomics 290, 387 (2015), Abstract; Full Text
Membrane localization of membrane type 1 matrix metalloproteinase by CD44 regulates the activation of pro-matrix metalloproteinase 9 in osteoclasts: M.A. Chellaiah, et al.; Biomed. Res. Int. 2013, Article ID 302392 (2013), Abstract; Full Text
Silver nanoparticles in therapeutics: development of an antimicrobial gel formulation for topical use: J. Jain, et al.; Mol. Pharm. 6, 1388 (2009), Abstract;
Actin polymerization modulates CD44 surface expression, MMP‐9 activation, and osteoclast function: V. Samanna, et al.; J. Cell. Physiol. 213, 710 (2007), Abstract;
Alpha-V-dependent outside-in signaling is required for the regulation of CD44 surface expression, MMP-2 secretion, and cell migration by osteopontin in human melanoma cells: V. Samanna, et al.; Exp. Cell. Res. 312, 2214 (2006), 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
