Matrix metalloproteinase-2 (MMP2) (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase), a member of the matrix metalloproteinase (MMP) enzyme family, is involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. MMP2 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Winchester syndrome, Torg syndrome and nodulosis-arthropathy-osteolysis syndrome. MMP2 is secreted as an inactive proenzyme/zymogen which is activated when cleaved by extracellular proteinases. The proform has a molecular weight of 72kDa and the active form 62kDa. A C-terminus peptide (aa. 475-490) was selected which is highly conserved and unique to MMP2, and is present in both pro- and active forms. The peptide was conjugated to KLH and use to immunize rabbits. The hyperimmune serum was affinity purified on a peptide-coupled sepharose column. The purified immunoglobulin recognizes 72 kDa and 66 kDa bands corresponding to MMP2 on Western immunoblots. Some tissue extracts also show MMP2 complexes and degradation products. Polyclonal MMP2/475 antibody immunostains MMP2 specifically in various tissue preparations including paraffin sections. This antibody has been marketed for many years by other companies and is now produced by EnCor Biotechnology Inc. The HGNC name for this protein is MMP2.
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