|Application ||IHC-P, IF, FC|
|Other Accession||2335, 203717|
|Isotype||Mouse / IgG1, kappa|
|Calculated MW||220kDa (monomer); 440kDa (dimer)|
|Other Names||Fibronectin, FN, Cold-insoluble globulin, CIG, Anastellin, Ugl-Y1, Ugl-Y2, Ugl-Y3, FN1, FN|
|Format||200ug/ml of Ab purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with 0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml.|
|Storage||Store at 2 to 8°C.Antibody is stable for 24 months.|
|Precautions||Fibronectin Antibody - Without BSA and Azide 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 dimeric glycoprotein of 440kDa, which is present in cells, extracellular matrix, and blood. It possesses at least four binding sites for collagen, glycosaminoglycans, transglutaminase, and a cell surface receptor. Fibronectin is involved in cell adhesion, tissue organization, and wound healing. This MAb is directed against the peptide core and reacts with both the plasma and cellular forms of fibronectin. It blocks the fibronectin-medicated cell attachment not by disrupting the collagen-fibronectin interaction, but by interfering with the attachment of fibronectin to its receptor on the cell surface.
Schoen RC, et. al. Hybridoma, 1982, 1(2):99-108
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