MMP-15

Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. They play critical roles in tissue remodeling, angiogenesis, tumor invasion, and rheumatoid arthritis. MMP15, also known as MT2MMP, is a membranetype MMP that is expressed in many tumor tissues including urothelial carcinoma, oral cancer, ovarian carcinoma, melanoma, and astrocytoma. Structurally, MMP15 consists of the following domains:a pro domain containing a furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexinlike domain, a transmembrane domain, and a cytoplasmic tail. Recombinant Human (rh) MMP15, consists of the pro domain, catalytic domain, hinge region and hemopexin-like domain. The pro domain contains the mutations R128P and R129G, which prevent activation by furin cleavage. Activation of rhMMP15 is possible by treatment with rhTrypsin.