Description of target: Matrix metalloproteinase-3 (MMP-3) also called stromelysin or transin, is a proteoglycanase closely related to collagenase (MMP1) with a wide range of substrate specificities. The complete primary structure for human MMP-3, which has 477 residues including a 17-residue signal peptide. MMP-3 and collagenase are 54% identical in sequence, suggesting a common origin for the evolution of the two proteinases. MMP-3 and collagenase expression are coordinately modulated in synovial fibroblast cultures. MMP-3 is a secreted metalloprotease produced predominantly by connective tissue cells. Together with other metalloproteases, it can synergistically degrade the major components of the extracellular matrix. It is capable of degrading proteoglycan, fibronectin, laminin, and type IV collagen, but not interstitial type I collagen. MMP-3 genotype may be an important determinant of vascular remodeling and age-related arterial stiffening, with the heterozygote having the optimal balance between matrix accumulation and deposition.;Species reactivity: Mouse;Application: ELISA;Assay info: ;Sensitivity: < 10 pg/mL
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Număr Catalog 247-OKBB00223CategorieAfaceri și industrie > Știință și laboratorFurnizorAviva Systems BiologyGentaurDimensiune96 TestsTipsingle
