
As the first member of membrane type (MT) MMPs, MMP-14, also known as MT1MMP, plays an important role in extracellular matrix (ECM) remodeling by being able to degrade type I collagen, activate pro MMP2 and process cell adhesion molecules such as CD44 and integrin αV. MMP-14 is therefore a key enzyme in many physiological and pathological processes such as angiogenesis and tumor invasion. Structurally, MMP14 consists of the following domains: a pro domain containing the furin cleavage site, a catalytic domain containing the zinc binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplamasic tail. Recombinant Human MMP-14 consists of the pro and catalytic domains, which can be activated by treatment with furin.

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