Invitrogen™ Human MMP9 ELISA Kit

Beschrijving

The Human Matrix Metalloproteinase 9 (Hu MMP-9) ELISA quantitates Hu MMP-9 in human serum, plasma, buffered solution, or cell culture medium. The assay will exclusivy recognize both natural and recombinant Hu MMP-9. Principle of the method The Human MMP-9 solid-phase sandwich ELISA (enzyme-linked immunosorbent assay) is designed to measure the amount of the target bound between a matched antibody pair. A target-specific antibody has been pre-coated in the wells of the supplied microplate. Samples, standards, or controls are then added into these wells and bind to the immobilized (capture) antibody. The sandwich is formed by the addition of the second (detector) antibody, a substrate solution is added that reacts with the enzyme-antibody-target complex to produce measurable signal. The intensity of this signal is directly proportional to the concentration of target present in the original specimen. Rigorous validation Each manufactured lot of this ELISA kit is quality tested for criteria such as sensitivity, specificity, precision, and lot-to-lot consistency. See manual for more information on validation.

MMP9 (matrix metallopeptidase 9, GELB, CLG4B) is a matrix metalloproteinase, a family of zinc and calcium-dependent endopeptidases that degrade extracellular matrix proteins. MMP9 is secreted as a 92kDa zymogen and cleavage of pro-MMP9 results in the active enzyme with a molecular weight of 82kDa. MMP9 has a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells, and is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 is supplied by bone marrow-derived cells and contributes to skin carcinogenesis. Further, MMP9 degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. Studies have shown that elevated MMP9 is associated with progression of idiopathic atrial fibrillation and aortic aneurysm.