大鼠纤连蛋白ELISA试剂盒描述：

       Fibronectin (FN), also known as LETS, is identified on the surface of fibroblasts by labeling with radioactive compounds or specific antibodies. FN is a 430,000-dalton dimeric glycoprotein that exists in two forms, called cellular and plasma fibronectin. Cellular and plasma fibronectins are heterodimers consisting of similar but not identical polypeptides. These two forms of FN differ in biologic activity. Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin and are involved in cell adhesion, cell motility, opsonization, would healing, and maintenance of cell shape. Because fibronectin stimulates endocytosis in several systems and promotes the clearance of particulate material from the circulation, it may function in the clearance of C1q-coated material such as immune complexes or cellular debris. FN, encoded on chromosome 8, has been implicated in tumorigenicity and cellular transformation, findings which are corroborated by fact that the rearrangement or modifications in the number of chromosome 8 have been associated with certain forms of cancer. The standard used in this kit is isolated from human plasma with the molecular mass of 200-250KDa. ScienCell's rat Fibronectin ELISA Kit is based on standard sandwich enzyme-linked immune-sorbent assay technology. Human Fibronectin-specific polyclonal antibodies are pre-coated onto 8 x 12 divisible strips. The human specific detection polyclonal antibodies re 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 into yellow after adding acidic stop solution. The intensity of yellow is proportional to the amount of rat Fibronectin captured in strips.

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       2. Bing, D. H.; Almeda, S.; Isliker, H.; Lahav, J.; Hynes, R. O. Fibronectin binds to the C1q component of complement.Proc. Nat. Acad. Sci. 79: 4198-4201, 1982.