Mouse TIMP‑1 Biotinylated 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.