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F7387

Sigma-Aldrich

Monoclonal Anti-Fibronectin antibody produced in mouse

clone FN-15, ascites fluid

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Synonym(s):
Anti-CIG, Anti-ED-B, Anti-FINC, Anti-FN, Anti-FNZ, Anti-GFND, Anti-GFND2, Anti-LETS, Anti-MSF, Anti-SMDCF
MDL number:
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

FN-15, monoclonal

contains

15 mM sodium azide

species reactivity

mouse, human, chicken

technique(s)

indirect ELISA: 1:5,000
indirect immunofluorescence: 1:200 using cultured human fibroblasts
microarray: suitable
western blot: 1:800

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... FN1(2335)
mouse ... Fn1(14268)

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This Item
F0791F6140F0916
conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

clone

FN-15, monoclonal

clone

IST-3, monoclonal

clone

FN-3E2, monoclonal

clone

IST-4, monoclonal

biological source

mouse

biological source

mouse

biological source

mouse

biological source

mouse

antibody form

ascites fluid

antibody form

ascites fluid

antibody form

ascites fluid

antibody form

ascites fluid

Gene Information

human ... FN1(2335)
mouse ... Fn1(14268)

Gene Information

human ... FN1(2335)

Gene Information

human ... FN1(2335)
mouse ... Fn1(14268)

Gene Information

human ... FN1(2335)

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General description

Fibronectin (FN) is an extracellular matrix protein composed of two nearly-identical disulfide-bound polypeptides with typical molecular weights of 220-280 kDa. Cellular fibronectin is structurally and antigenically similar to cold insoluble globulin from plasma and antibodies to either form usually cross-react. Careful analysis of the FN molecule indicates that it contains several functionally and structurally distinct domains which may bind to cell surfaces and to a variety of molecules such as collagen, heparin, gelatin, fibrin and DNA. FN′s play an important role in diverse biological phenomena including cell adhesion, cell migration, hemostasis and thrombosis, wound healing and the ability to induce a more normal phenotype in transformed cells.
Monoclonal Anti-Fibronectin (mouse IgG1 isotype) is derived from the hybridoma produced the fusion of mouse myeloma cells and splenocytes from immunized mice. Fibronectin (FN) belongs to glycoprotein family widely expressed in many tissues. FN is an extracellular matrix protein composed of two nearly-identical disulfide-bound polypeptides with typical molecular weights of 220-240 kDa. There are three isoforms of fibronectin, that includes cellular FN, plasma FN and fetal FN. Cellular fibronectin is structurally and antigenically similar to cold insoluble globulin from plasma and antibodies to either form usually cross-react. Careful analysis of the FN molecule indicates that it contains several functionally and structurally distinct domains which may bind to cell surfaces and to a variety of molecules such as collagen, heparin, gelatin, fibrin and DNA. FN gene in human chromosome is mapped to 2q35.
Mouse monoclonal clone FN-15 anti-Fibronectin antibody labels fibronectin in the pericellular extracellular matrix of cultured human fibroblasts using indirect immunofluorescent methods. It also labels fibronectin in chicken and mouse cells. The FN-15 antibody specifically stains fibronectin in immunoblotting, and in an ELISA is reactive with human plasma fibronectin.

Immunogen

fibronectin from human plasma

Application

Monoclonal Anti-Fibronectin may be used to specifically localize fibronectin in human cell culture and in tissue sections by immunoblotting, immunohistochemical techniques and to stain fibronectin in hydrogels.
Mouse monoclonal clone FN-15 anti-Fibronectin antibody may be used to specifically localize fibronectin in human cell culture and in tissue sections by immunoblotting and immunohistochemical techniques. Monoclonal antibodies reacting specifically with FN may be used to localize FN in human cell cultures, in tissue sections and in plasma.

Biochem/physiol Actions

Fibronectin (FN) play an important role in diverse biological phenomena including cell adhesion, cell migration, hemostasis and thrombosis, wound healing and the ability to induce a more normal phenotype in transformed cells. FN is upregulated in many cancers. FN increases the expression of matrix metalloproteinases (MMPs), promoting cancer cell invasion and metastasis.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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Intracellular signaling cascades triggered by the NK1 fragment of hepatocyte growth factor in human prostate epithelial cell line PNT1A
Pavone LM, et al.
Cellular Signalling, 23(12), 1961-1971 (2011)
Modulus-driven differentiation of marrow stromal cells in 3D scaffolds that is independent of myosin-based cytoskeletal tension
Parekh SH, et al.
Biomaterials, 32(9), 2256-2264 (2011)
Expression of fibronectin in esophageal squamous cell carcinoma and its role in migration
Xiao J, et al.
BMC Cancer, 18(1), 976-976 (2018)
Hansong Du et al.
Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 36(5), 1821-1834 (2015-07-18)
To explore the explicit role of fibronectin (FN) isforms in atherosclerotic lesions and the underlying mechanisms. Inducible stable expression was performed, and similar results were observed between EDA+FN (FN containing EDA domain) and EDA-FN (FN devoid of EDA domain). FN
Cécile Milet et al.
Scientific reports, 7(1), 16153-16153 (2017-11-25)
Beige adipocyte differentiation within white adipose tissue, referred to as browning, is seen as a possible mechanism for increasing energy expenditure. The molecular regulation underlying the thermogenic browning process has not been entirely elucidated. Here, we identify the zinc finger

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