Matrix Metalloproteinase-7 human

One unit of enzyme activity is defined as the digestion of 1 μg of azocoll/min. at pH 7.5 and 37 °C.

Matrix metalloproteinase-7 (MMP7) human has been used in in silico analysis of MMP-7 proteolysis of perlecan.

Matrix metalloproteinase-7 (MMP-7) catalyzes the cleavage of extracellular matrix (ECM) proteins such as proteoglycans, fibronectin, entactin, laminin, collagen III/ IV/ V/ IX/ X/ XI, type I/ II/ IV/ V gelatins, and elastin. Matrix metalloproteinase-7 facilitates initial stages of tumor progression. Activated MMP7 plays a vital role in human colorectal cancer (CRC) liver metastases. Overexpression of MMP7 is observed in various human cancers, such as breast, lung, prostate, esophagus, stomach, endometrium, and ovarian carcinomas, as well as esophageal squamous cell carcinomas. Increased expression of MMP7 is also associated with pathogenesis of demyelinating multiple sclerosis (MS) lesions. Both in silico and in vitro studies show that MMP7 degrades glycosylated and basement membrane bound perlecan and plays a vital role in prostate cancer cell invasion.

Matrix metalloproteinase-7 (MMP7) also referred to as matrilysin is encoded by the gene mapped to human chromosome 11q21-q22. MMP7 is a smallest member of MMP enzyme family and is highly expressed in cancer cells. MMP7 is exclusively released by epithelial cells.

Solution in 10 mM HEPES, 5 mM CaCl₂, 150 mM NaCl