Matrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in arthritis, periodontitis, and metastasis. The activation and activity of MMPs are regulated by a family of endogenous inhibitors, tissue inhibitors of metalloproteinase (TIMP). TIMP2 (also called CSC-21K) is a 24 kDa glycoprotein that is expressed by a variety of cell types. It forms a non covalent, stoichiometric complex with both latent and active MMPs. TIMP2 shows a preference for MMP2. TIMPs are capable of altering the metastatic potential of cancer cells and have been shown to inhibit invasion and metastasis in animal models. TIMP2 is constitutively produced in low (pg/ml) levels by most cell types in tissue culture. The low protein levels produced often require concentration of cell culture media to visualize the bands by Western Blotting.

Secreted