|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||262625 Da|
|Other Names||Fibronectin, FN, Cold-insoluble globulin, CIG, Anastellin, Ugl-Y1, Ugl-Y2, Ugl-Y3, FN1, FN|
|Target/Specificity||A recombinant protein was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|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.
Fibronectins are high molecular weight glycoproteins. Found in plasma or at the cell surface, fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Additionally, binding of fibronectin to collagen, fibrin, heparin, DNA, and actin (1) may trigger key events such as cell migration and repair during the early phases of wound healing (1-3).
1. Yamada,K.M. (1983) Annu. Rev. Biochem., 52, 761-799.
2. Hynes,R.O. and Yamada,K.M. (1982) J. Cell. Biol., 95, 369-377.
3. Skorstengaard,K., Thogersen,H.C., Vibe-Pedersen,K., Petersen,T.E. and Magnusson, S. (1982) Eur. J. Biochem., 128, 605-623
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