Anti-Fibronectin/FN1 Antibody Picoband® Fluoro488 Conjugated

Fibronectin is a high-molecular weight glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. It is mapped to 2q35. This gene encodes fibronectin, a glycoprotein present in a soluble dimeric form in plasma, and in a dimeric or multimeric form at the cell surface and in extracellular matrix. The encoded preproprotein is proteolytically processed to generate the mature protein. Fibronectin is involved in cell adhesion and migration processes including embryogenesis, wound healing, blood coagulation, host defense, and metastasis. The gene has three regions subject to alternative splicing, with the potential to produce 20 different transcript variants, at least one of which encodes an isoform that undergoes proteolytic processing. The full-length nature of some variants has not been determined.

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.

Angiogenesis, Cancer, Cardiovascular, Cell Biology, Cytoskeleton/ECM, ECM Enzymes, Extracellular Matrix, Invasion/Microenvironment, Protease Inhibitors, Proteolysis/Ubiquitin, Signal Transduction

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. Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.

1. 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. 2. Castelletti, F., Donadelli, R., Banterla, F., Hildebrandt, F., Zipfel, P. F., Bresin, E., Otto, E., Skerka, C., Renieri, A., Todeschini, M., Caprioli, J., Caruso, M. R., Artuso, R., Remuzzi, G., Noris, M. Mutations in FN1 cause glomerulopathy with fibronectin deposits. Proc. Nat. Acad. Sci. 105: 2538-2543, 2008.