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Description
Purified anti-MMP3. MMP3 is a member of the matrix metalloproteinase family proteins (MMPs). Members of this family are structurally related to zinc-containing enzymes that degrade the extracellular matrix (ECM), connective tissue proteins in normal physiological processes such as embryonic development, reproduction, and tissue remodeling, and in disease processes such as arthritis and metastasis as well. MMP3 consists of a prodomain that is cleaved upon activation, a catalytic domain containing the zinc binding site, a short hinge region, and a carboxyl terminal (hemopexin-like repeats) domain. Substrates of MMP3 include 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 is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. Also, it has been known that a polymorphism in the MMP3 promoter region is associated with the risk of coronary heart disease and myocardial infarction due to lower MMP3 proteolytic activity and higher ECM deposition in atherosclerotic lesions.
Immunogen
Recombinant human MMP-3, amino acids Tyr18 -Cys477, was expressed with N-terminal His9-SGGGSGGGIEGR tag in 293E cells.
Other Names
Progelatinase, STR1, Transin, Stromelysin I, MMP-3, Transin-1, STMY1, SL-1, CHDS6