The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-3, MMP-10 and MMP-11 (also designated stromelysin-1, 2 and 3, respectively) activate procollagenase. MMP-3 activation of procollagenase can occur via two pathways. Direct activation by MMP-3 is slow and activation by MMP-3 in conjunction with tissue or plasma proteinases is rapid. MMP-10 is expressed in small intestine, and at lower levels in lung and heart. MMP-11 is specifically expressed in stromal cells of breast carcinomas and contributes to epithelial cell malignancies.
Immunohistochemistry (Formalin-fixed) (1-2µg/ml for 30 minutes at RT)(Staining of formalin-fixed tissues requires heating tissue sections in 10mM Tris with 1mM EDTA, pH 9.0, for 45 min at 95&degC followed by cooling at RT for 20 minutes),
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