MMP-13 (activated) ELISA

Matrix metalloproteinases (MMPs) comprise a family of secreted and membrane-bound endopeptidases which hydrolyze extracellular matrix proteins. Based on their preferred substrates and on structural features MMPs can be divided into collagenases, gelatinases, stromelysins and membrane-type matrix metalloproteinases. Their activity is tightly regulated by inhibitors. Collagenase 3 (MMP-13) is a secreted 452 residue protein which is released from cells as an inactive zymogen and activated extracellularly by removal of its propeptide. Cleavage of the 84 residue propeptide can be catalysed by other MMPs such as MMP-2 and MMP-14, or by factors like plasmin. Under normal conditions, MMP-13 is expressed during embryogenesis (fetal bone development) and is present only at very low levels in adult tissue. However, this enzyme is reported to be involved in the development and metastasis of breast and lung carcinomas, chondrosarcomas and osteosarcomas, head and neck carcinomas and some forms of skin cancer. Additionally, this enzyme plays an important role in degenerative bone diseases including osteoarthritis and rheumatoid arthritis.