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Matrix metalloproteinases (MMP′s) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMP′s share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an ~10 kDa segment from the N terminus and they are inhibited by tissue inhibitor of metalloproteinases (TIMP). These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in arthritis, periodontitis, and metastasis.MMP-9 (Gelatinase B, 92 kDa gelatinase/type IV collagenase) is secreted as a 92 kDa zymogen which is proteolytically processed to the 83 kDa active form; a 68 kDa has also been detected. MMP-9, along with its most closely related member of the MMP family, MMP-2, show substrate specificity toward type IV and V collagens, gelatin and elastin. Numerous studies have shown a correlation between collagenase expression and metastatic potential. Elevated levels of MMP-9 in plasma suggest that it may be a useful marker for the diagnosis or prognosis of cancer in general.,官网链接:https://www.sigmaaldrich.cn/product/mm/im09l
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