444217
MMP-3, Catalytic Domain, Human, Recombinant, E. coli
Synonym(s):
Matrix Metalloproteinase 3, Stromelysin-1, Catalytic Domain
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assay
≥90% (SDS-PAGE)
Quality Level
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
General description
Note: 1 mU = 1 milliunit.
Recombinant, human MMP-3 catalytic domain expressed in E. coli.
Warning
Toxicity: Standard Handling (A)
Unit Definition
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.
Physical form
In 50 mM Tris-HCl, 10 mM CaCl₂, 1 µM ZnCl₂, 0.05% NaN₃, pH 7.5.
Reconstitution
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.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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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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