Anti-Human MMP-3 Antibody

Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP3 (stromelysin1), can degrade a broad range of substrates including collagen α chains, aggrecan, laminin, fibronectin, elastin, casein, α1 antitrypsin, myelin basic protein, IL1β, IGFBP3, pro MMP1, pro MMP7, pro MMP8, pro MMP9 and pro MMP13. MMP3 does not cleave the triple helical region of interstitial collagens, a characteristic which distinguishes the stromelysins from the collagenases. The MMP3 substrate repertoire extends beyond extracellular matrix proteins and implicates MMP3 in roles other than direct tissue remodelling, for instance, enzyme cascades and cytokine regulation. MMP3 is expressed by fibroblasts, chrondrocytes, osteoblasts, endothelial cells, smooth muscle cells and macrophages. Structurally, MMP3 may be divided into several distinct domains; a prodomain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexinlike) domain.