Human TIMP‑4 Biotinylated Antibody

Tissue inhibitors of metalloproteinases (TIMPs) are a family of secreted proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs). There are four known members of the family, TIMP-1, -2, -3 and -4. TIMP-4 is produced by a wide range of tissues, particularly brain, heart, ovary and skeletal muscle (1, 2). Limited studies have shown that TIMP-4 has a tumor suppressive effect against Wilm’s tumor, exhibits negative correlation with glioma maligancy and is found in breast carcinoma cells (3 - 5). TIMP-4 inhibits MMP-mediated proteolysis by forming a non-covalent binary complex with the MMP active site through its N-terminal domain. In addition, it binds to the hemopexin-like domain of pro-MMP-2 through its C-terminal domain in a manner similar to TIMP-2 (6). However, unlike TIMP-2, TIMP-4 does not promote pro-MMP-2 activation by MT1-MMP (MMP-14) (7). Although TIMP-4 is a potent inhibitor of most MMPs, it is not an effective inhibitor of ADAMs, such as TACE (8, 9).