Recombinant Human MMP-2

Matrix metallopeptidase 2, also known as MMP2, is an enzyme involved in the 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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP-2 degrades type IV collagen, the major structural component of basement membranes and plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP2 has been found to be associated with tumor invasion in various cancers.¹

The biological activity of Human MMP-2 was determined by its ability to cleave a fluorogenic 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 > 1,000 pmoles/min/μg.

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Ala30

Lyophilized

The predicted molecular weight of Recombinant Human MMP-2 is Mr 71 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is Mr 69 kDa.

71

The protein was 0.2 μm filtered and lyophilized from a solution of 25 mM Mes, 10 mM CaCl₂, 150 mM NaCl, 0.05% Brij-35, pH 5.5.

This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.

Next Day Ambient

1. Viswanadha, VP. et al. (2017) J Cell Biochem. 118(9):2865-2876.