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Matrix Metalloproteinase 3 (MMP3), also referred to as stromelysin-1, is a 378 amino acid zinc- and calcium-dependent protease expressed by fibroblasts, endothelial cells, macrophages, osteoblasts, chondrocytes, vascular smooth muscle cells, and keratinocytes. MMP3 is secreted as a pro-enzyme (pro-MMP3) and is activated by proteolytic cleavage by serine proteases such as plasmin. The substrates for MMP3 are collagen type III, IV and V, proteoglycans, laminin, fibronectin, fibrillin, osteopontin, and gelatin. MMP3 is mainly implicated in rheumatoid arthritis disease in which it is involved in degradation of connective tissue in the synovial joint. MMP3 levels increased in serum in patients with rheumatoid arthritis disease, osteoarthritis of the hip, and certain tumors.
AlphaLISA technology allows the detection of molecules of interest in a no-wash, highly sensitive, quantitative assay. In an AlphaLISA assay, a biotinylated anti-analyte antibody binds to the Streptavidin-coated Donor beads while another anti-analyte antibody is conjugated to AlphaLISA Acceptor beads. In the presence of the analyte, the beads come into close proximity. The excitation of the Donor beads causes the release of singlet oxygen molecules that triggers a cascade of energy transfer in the Acceptor beads, resulting in a sharp peak of light emission at 615 nm.
|Assay Target Class||Protein|
|Experimental Type||In vitro|
|Product Brand Name||AlphaLISA|
|Shipping Condition||Blue Ice|
|Unit Size||500 assay points|
The AlphaLISA® assay is a homogeneous immunoassay alternative to classical ELISA. AlphaLISA assays were originally utilized to detect analytesin cell cultures upernatants or serum/plasma samples.