Recombinant Human MMP-9

Matrix metallopeptidase 9, also known as MMP9, is a biological enzyme that is a member of the matrix metalloproteinases (MMPs). MMP9 is thought to play a critical role in tumor cell invasion,¹ breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. MMP-9 is secreted from cells and, once activated, is thought to degrade collagen in the extracellular matrix.² MMP-9 is one of the major proteases produced by osteoclasts and possibly plays a role in osteoclastic bone resorption.³

The biological activity of Human MMP-9 was determined by its ability to cleave a fluorescent peptide substrate, (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-(3-[2, 4-dinitrophenyl]-L-2, 3-diaminopropionyl)-Ala-Arg-NH2. The specific activity, measured under the described conditions, is > 1,300 pmoles/min/μg.

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Ala20

Solution

The predicted molecular weight of Recombinant Human MMP-9 is Mr 77 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is Mr 93 kDa.

77

The protein is 0.2 μm filtered and provided as a solution in 50 mM Tris, 10 mM CaCl₂, 150 mM NaCl, 0.05% Brij-35, pH 7.5.

Next Day 2-8°C

1. Viswanadha, VP. et al. (2017) J Cell Biochem. 118(9):2865-2876.
2. Mobashery, S. et al. (1995) Cancer Res. 55: 2548
3. Tökés, ZA.et al. (1995) J Neurochem. 64: 1312
4. Kumegawa, M. et al. (1994) J Biol. Chem. 269: 15006