rh-Polypeptide-15 is a single chain recombinant human peptide, produced by fermentation in E. coli. The starting gene is directly isolated from a human cell which codes for Tissue Inhibitor of Metalloproteinases-2. It contains a maximum of 220 amino acids
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.
TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMP family members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.
