The Matrix metalloproteinase-14 (MMP-14) belongs to a family of zinc-dependent endopeptidases. The ability of MMP-14 to degrade type I collagen, and activate pro-MMP-2 and pro-MMP-9 makes it a key enzyme in many physiological and pathological processes such as angiogenesis and tumor invasion. MMP-14 is structurally a multi-domain metalloenzyme, composed of a prodomain, a metal-binding catalytic domain, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplamasic tail. The catalytic, and hinge domains of MT1-MMP were expressed in Escherichia coli and the active form was generated by successive autoproteolysis of the N- and C-terminal sites during refolding. MW: ~ 24.0 kDa (112-318 aa). Purity ≥90%