Anti-MMP3 / Matrix Metalloproteinase 3, clone MMP3/2655

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide. 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. MMP3, MMP10 and MMP11 (also designated stromelysin-1, 2 and 3, respectively) activate procollagenase. MMP3 activation of procollagenase can occur via two pathways. Direct activation by MMP3 is slow and activation by MMP3 in conjunction with tissue or plasma proteinases is rapid. MMP10 is expressed in small intestine, and at lower levels in lung and heart. MMP11 is specifically expressed in stromal cells of breast carcinomas and contributes to epithelial cell malignancies. Protein function: Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V, collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. [The UniProt Consortium]