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Description

Matrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMPs share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an approximately 10 kDa segment from the N-terminus and their activity is regulated by endogenous inhibitors. 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). TIMP-1 (also called EPA, Fibroblast collagenase inhibitor or collagenase inhibitor) is a 28 kDa glycoprotein that is expressed by a variety of cell types. It forms a non-covalent, stoichiometric complex with both latent and active MMPs. TIMP-1 preferentially binds and inhibits MMP-9. TIMPs are capable of altering the metastatic potential of cancer cells and have been shown to inhibit invasion and metastasis in animal models., This Anti-TIMP-1 (Ab-1) Mouse mAb (7-6C1) is validated for use in Immunoblotting, Immunocytochemistry, Paraffin Sections for the detection of TIMP-1 (Ab-1)., Recognizes the ~28.5 kDa TIMP-1 protein. Also recognizes MMP/TIMP-1 complexes., Purified mouse monoclonal antibody (see application references). Recognizes the ~28 kDa TIMP-1 protein.