To establish the most effective formula, the MMP inhibitory activities of doxycycline, commercial seed extract (Finzelberg, Germany), commercial leaf extract (Dr. Willmar Schwabe, Germany) and ALH-L1005 were estimated experimentally. Before the MMP assay, recombinant human MMP-2 and MMP-9 (R&D Systems, USA) were activated with 1 mM APMA. The MMP activities were measured on a spectrofluorometer (Perkin-Elmer, USA) using 2,4-dinitrophenyl-Pro-Leu-Gly-Met-Trp-Ser-Arg (Calbiochem, USA) as a substrate. The MMP (10 nM) and substrate (1 µM) were mixed in 2 mL of reaction buffer (50 mM Tricine, pH 7.5, 10 mM CaCl2, 200 mM NaCl) along with each test material. Fluorescence intensity was measured at room temperature using a 280 nm excitation wavelength and a 360 nm emission wavelength.
Recombinant human mmp 2 and mmp 9
Manufactured by R&D Systems
Sourced in United States
Recombinant human MMP-2 and MMP-9 are recombinant protein products produced in E. coli. MMP-2 and MMP-9 are members of the matrix metalloproteinase (MMP) family of enzymes that are involved in the degradation of extracellular matrix components.
Automatically generated - may contain errors
Lab products found in correlation
2 protocols using recombinant human mmp 2 and mmp 9
1
Comparative MMP Inhibition Assay
2
Fluorometric Assay for MMP Activity
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MMP activity was measured using an LS50B spectrofluorometer (Perkin-Elmer, Waltham, MA, USA) using the substrate 2,4-dinitrophenyl-Pro-Leu-Gly-Met-Trp-Ser-Arg (Calbiochem, San Diego, CA, USA), as previously described [13 (link)]. Recombinant human MMP-2 and MMP-9 were purchased from R&D Systems (Minneapolis, MN, USA) and used after activation with 1 mM APMA (amino-phenyl mercuric acetate) before the assay. MMP (10 nM) and substrate (1 μM) were mixed in 2 ml of reaction buffer (50 mM Tricine, pH 7.5, 10 mM CaCl2, 200 mM NaCl) in the presence or absence of ALS. Fluorescence intensity was measured at room temperature using a 280-nm excitation wavelength and a 360-nm emission wavelength.
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