444217
MMP-3, Catalytic Domain, Human, Recombinant, E. coli
别名:
Matrix Metalloproteinase 3, Stromelysin-1, Catalytic Domain
assay
≥90% (SDS-PAGE)
form
liquid
specific activity
≥1250 mU/mg protein
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze, avoid repeated freeze/thaw cycles
foreign activity
other MMP activity, none detected
shipped in
wet ice
storage temp.
−70°C
Quality Level
General description
Note: 1 mU = 1 milliunit.
Recombinant, human MMP-3 catalytic domain expressed in E. coli.
Physical form
In 50 mM Tris-HCl, 10 mM CaCl₂, 1 µM ZnCl₂, 0.05% NaN₃, pH 7.5.
Preparation Note
Following initial thaw, aliquot and freeze (-70°C).
Other Notes
Nagase, H., et al. 1994. J. Biol. Chem. 269, 20952.
Wilhelm, S.M., et al. 1993. J. Biol. Chem. 268, 21906.
Ye, Q.Z., et al. 1992. Biochemistry 31, 11231.
Wilhelm, S.M., et al. 1993. J. Biol. Chem. 268, 21906.
Ye, Q.Z., et al. 1992. Biochemistry 31, 11231.
One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol MCA-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(DNP)-NH₂ per min at 37°C, pH 7.0.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Lise Boon et al.
The FEBS journal, 286(5), 930-945 (2018-11-14)
Matrix metalloproteinases (MMPs) are secreted as proenzymes, containing propeptides that interact with the catalytic zinc, thereby controlling MMP activation. The MMP-9 propeptide is unique in the MMP family because of its post-translational modification with an N-linked oligosaccharide. ProMMP-9 activation by
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