Matrix metalloproteinase-3 (MMP-3) also called stromelysin or transin, is a proteoglycanase closely related to collagenase (MMP-1) with a wide range of substrate specificities. The complete primary structure for human MMP-3 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. The standard product used in this kit is recombinant human MMP-3, consisting of 460 amino acids with a molecular mass of 52 kDa. The detected MMP-3 includes zymogen and active enzyme.

ScienCell's human MMP-3 ELISA kit is based on standard sandwich enzyme-linked immune-sorbent assay technology. Human MMP-3-specific polyclonal antibodies are pre-coated onto 8 x 12 divisible strips. The human-specific detection polyclonal antibodies are biotinylated. The test samples and biotinylated detection antibodies are subsequently added to the wells and then washed with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex is added and unbound conjugates are washed away with PBS or TBS buffer. HRP substrate TMB is used to visualize HRP enzymatic reaction. TMB is catalyzed by HRP to produce a blue color product that changes to yellow after adding acidic stop solution. The intensity of yellow is proportional to the amount of human MMP-3 in the sample that is captured on the strips.