TIMP-1 human

TIMP1 (tissue inhibitor of metalloproteinase 1) is a glycoprotein and is a member of TIMP family of endogenous MMP (matrix metalloproteinase) inhibitors. Humans contain four TIMPs. All TIMPs contain an N-terminal of 125 residues, a 65-residue C-terminal, and both these domains contain three disulfide bonds. The N-terminal domain inhibits MMPs by folding into a separate unit. TIMP1 is encoded by the gene mapped to human chromosome Xp11.23.

TIMP1 functions as a poor inhibitor of MT1 (membrane type 1)-MMP, MT3-MMP, MT5-MMP and MMP-19. It inhibits ADAM10 (a disintegrin and metalloproteinase domain-containing protein 10) protein. In human umbilical vein endothelial cells (HUVECs), the down-regulation of TIMP1 and up-regulation of MMP-3 results in aberrant endothelium-dependent vasodilation, EC (endothelial cell) death, and endothelial interruption in a FOXO3 (forkhead box O3)-mediated manner. In patients with CAD (coronary artery disease) and acute coronary syndrome (ACS), the urine levels of this protein are elevated. This protein interacts with Bcl-2 (B cell lymphoma) protein, and induces apoptosis in lung adenocarcinoma cells. The plasma levels of this protein are increased in patients with obesity and obesity-related disorders, such as steatosis, where it participates in pathogenesis of diet-induced hepatic steatosis and glucose intolerance.

In 50 mM Tris-HCl, pH 7; 200 mM NaCl; 5 mM CaCl?; 1 ?M ZnCl?; 0.05% Brij^® L23; 0,05% NaN?

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