Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Interacts (via the C-terminal) with MMP2 (via the C-terminal PEX domain); the interaction inhibits the MMP2 activity. Predominantly expressed in the lung in alveolar macrophages and epithelial cells. Also found in brain, kidney, intestine, spleen and heart. The activity of TIMP2 is dependent on the presence of disulfide bonds. Belongs to the protease inhibitor I35 (TIMP) family.