General description
Native MMP-2 from mouse calvariae. Pro-MMP-2 (progelatinase A) is cleaved in vivo by MT2-MMP to yield a 67 kDa intermediate and the 62 kDa active enzyme.
Native MMP-2 from mouse calvariae. Pro-MMP-2 (progelatinase A) is cleaved in vivo by MT2-MMP to yield a 67 kDa intermediate and the 62 kDa active enzyme. Matrix metalloproteinase-2 (MMP-2) is involved in the degradation of several components of the extracellular matrix under various pathological conditions. In cancer tissues, MMP-2 is secreted by a proenzyme (proMMP-2), which is activated by membrane type 2 matrix metalloproteinase (MT2-MMP) on the cell surface. The 72 kDa pro-MMP-2 (progelatinase A) is cleaved by MT2-MMP to yield a 67 kDa intermediate and the 62 kDa active enzyme. Useful for immunoblotting, substrate cleavage assays, and zymography. Product may contain variable trace amount of active MMP-2.
Unit Definition
One unit is defined as the amount of enzyme that can hydrolyze 1 μmol of the substrate N-(2,4)-DNP-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min at 37°C, pH 7.0.
Physical form
In 200 mM NaCl, 50 mM Tris-HCI, 5 mM CaCl₂, 1 μM ZnCl₂, 0.05% Brij®-35 Detergent, pH 7.0.
Reconstitution
Following initial thaw, aliquot and freeze (-70°C).
Legal Information
Brij is a registered trademark of Croda International PLC
Certificates of Analysis (COA)
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C G Knight et al.
FEBS letters, 296(3), 263-266 (1992-01-27)
(7-methoxycoumarin-4-yl)Acetyl-Pro-Leu-Gly-Leu-(3-[2,4-dinitrophenyl]-L- 2,3-diaminopropionyl)-Ala-Arg-NH2 (Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2) has been synthesised as a fluorogenic substrate for the matrix metalloproteinases. The highly fluorescent 7-methoxycoumarin group is efficiently quenched by energy transfer to the 2,4-dinitrophenyl group. The punctuated metalloproteinase (PUMP, EC 3.4.24.23) cleaves the substrate at the
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