For research use only. Not for use in diagnostic procedures.
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MMP-7 (Matrylisin) is a proteolytic enzyme belonging to Matrix Metalloproteinase (MMPs) family which consists of 24 known human zinc and calcium proteases with essential roles in breaking down components of the extracellular matrix (ECM). MMPs share common structural motifs including a pro-peptide domain, a catalytic domain, a hinge region, and a hemopexin-like domain. Synthesized as pro-enzymes, most MMPs are secreted before conversion to their active form. Structurally, MMP-7 is the smallest of the MMPs and consists of two domains: a pro-domain that is cleaved upon activation and a catalytic domain containing the zinc-binding site which can degrade a wide range of extracellular matrix including collagen IV and X, gelatin, casein, laminin, aggrecan, entactin and elastin and also activate several other MMPs. MMP-7 is expressed in epithelial cells of normal and diseased tissues and plays key roles in connective tissue remodeling and cancer metastasis.
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|
|Shipping Condition||Blue Ice|
|Unit Size||100 assay points|