|Application ||WB, IHC|
|Calculated MW||262625 Da|
|Application & Usage||Western blotting (0.5 – 2.0 µg/ml), Immunohistochemistry (20-40 µg/ml). However, the optimal concentrations should be determined individually.|
|Other Names||Fibronectin, FN, Cold-insoluble globulin, CIG, Anastellin, Ugl-Y1, Ugl-Y2, Ugl-Y3, FN1, FN|
|Formulation||100 µg (0.5mg/ml) antigen affinity purified rabbit anti-Fibronectin polyclonal antibody in phosphate-buffered saline (PBS) containing 50% glycerol, 0.1% BSA and 0.02% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||Fibronectin Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.|
|Cellular Location||Secreted, extracellular space, extracellular matrix|
|Tissue Location||Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine.|
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Provided below are standard protocols that you may find useful for product applications.
Fibronectin is a glycoprotein synthesized in the liver for the circulating blood plasma form, and is synthesized by many mesenchymal cells, for the extracellular matrix form. It is composed of two similar, but not identical protein chains, which are linked by two disulfide linkages at the C-terminal end of the chains. The chains are composed of domains which have specific secondary structures linked together by regions which are especially susceptible to proteolytic action. For this reason, detection by immunoblot (western) may show considerable variability in the observed apparent molecular weights, which is predicated on the source of the fibronectin, and to what degree proteolysis has occurred. Bands approximately 225 kDa should be observed after SDS-PAGE when reducing and denaturing conditions are used
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