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444217

Sigma-Aldrich

MMP-3, Catalytic Domain, Human, Recombinant, E. coli

Synonym(s):

Matrix Metalloproteinase 3, Stromelysin-1, Catalytic Domain

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352202
NACRES:
NA.77

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.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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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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