|Application ||WB, IHC, IF, FC, IP, E|
|Reactivity||Human, Mouse, Rat, Pig|
|Calculated MW||220kDa (monomer); 440kDa (dimer)|
|Other Names||Fibronectin, FN, Cold-insoluble globulin, CIG, Anastellin, Ugl-Y1, Ugl-Y2, Ugl-Y3, FN1, FN|
|Target/Specificity||T-cell lymphoma biopsy|
|Application Note||ELISA : For coating, order Ab without BSA|
Flow Cytometry : 0.5-1ug/million cells
Immunofluorescence : 0.5-1.0 µg/ml
Western Blotting : 0.5-1.0 µg/ml
Immunoprecipitation : 0.5-1 µg/500ug protein lysate
Immunohistology (Frozen & Formalin-fixed) : 0.5-1.0 µg/ml for 30 minutes at RT
(Staining of formalin-fixed tissues requires boiling tissue sections in 10mM citrate buffer, pH 6.0, for 10-20 min followed by cooling at RT for 20 minutes).
|Format||0.5 ml at 200ug/ml with BSA and azide|
|Storage||Store at 2 to 8°C.Antibody is stable for 24 months.|
|Precautions||Fibronectin Antibody - With 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 an extracellular matrix glycoprotein present on most cell surfaces, in extracellular fluids and in plasma. A high molecular weight heterodimeric protein, it was originally discovered as a protein missing from the surfaces of virus-transformed cells, and it has been shown to be involved in various functions including cell adhesion, cell motility and wound healing. Alternative splicing and glycosylation give rise to several different forms of Fibronectin, some of which exhibit restricted tissue distribution or association with malignancies. It has been shown that Myofibroblast phenotype formation correlates with the occurrence of glycosylated Fibronectin and Fibronectin splice variants in Dupuytren’s disease.
1. Epstein AL, et. al. Cancer Research, 1995, 55(12):2673-80.
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