Tissue Inhibitor of Metalloproteinase-2 人

Tissue inhibitor of metalloproteinase-2 (TIMP-2) is an extracellular inhibitor of matrix metalloproteinases (MMPs). There are six conserved cysteine residues forming disulfide loops in its amino- and carboxy-terminal domains. The gene encoding this protein is localized on human chromosome 17q25.

Tissue inhibitor of metalloproteinase-2 (TIMP-2), like other protease inhibitors, functions as a key modulator of extracellular matrix degradation during tissue development and remodeling. TIMP-2 can also act through a matrix metalloproteinase (MMP)-independent mechanism inhibiting endothelial cell proliferation in vitro. It demonstrates anti-angiogenic activities in vivo. TIMP-2 is a target gene of the microRNA-miR-22.

TIMP-2 has a greater binding efficiency to MMP-2 than the other MMPs. Although TIMP-2 is an inhibitor of MMP-2, it is also required at low concentrations for the activation of MMP-2.

Lyophilized from a 0.2 μm filtered solution in 25 mM Tris, and 150 mM sodium chloride, pH 7.5.

The biological activity is measured by the ability to inhibit human MMP-2 hydrolysis of a fluorogenic MMP substrate.