Mouse TIMP‑1 Antibody

Tissue inhibitors of metalloproteinases or TIMPs are a family of homologous proteins that regulate the activity of matrix metalloproteinases (MMPs) (1, 2). There are four known members of the family, TIMP-1, TIMP-2, TIMP-3, and TIMP-4 that have been found to exhibit multiple functions, including inhibition of active MMPs, pro-MMP activation, cell growth promotion, matrix binding, inhibition of angiogenesis, and the induction of apoptosis. Structurally, TIMPs have two domains, an N‑terminal domain and a C-terminal domain. Each domain consists of three disulfide-bonded loops. TIMP-1 is a glycoprotein produced by a wide range of cell types. Through its N-terminal domain, TIMP-1 inhibits active MMPs by forming a non-covalent binary complex with the MMP active site. The C-terminal domain of TIMP-1 interacts with the C-terminal domain of pro-MMP-9, which may play a role in regulating pro-MMP-9 activation.