Invitrogen

Fibronectin Polyclonal Antibody

View all (101) Fibronectin antibodies
Datasheet
Protocols
Questions & Answers
Datasheet
Protocols
Questions & Answers

Product Details

PA5-99457

Applications
Tested Dilution
Publications

Western Blot (WB)

1:500-1:2,000
-

Immunohistochemistry (Paraffin) (IHC (P))

1:50-1:200
-

Immunocytochemistry (ICC/IF)

1:100-1:500
-
Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

A synthesized peptide derived from human FN1(Accession P02751), corresponding to amino acid residues Q2352-E2386.
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Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

Affinity chromatography

Storage buffer

PBS, pH 7.4, with 50% glycerol

Contains

0.02% sodium azide

Storage conditions

-20°C

Shipping conditions

Wet ice

RRID

AB_2818390

Product Specific Information

Antibody detects endogenous levels of total Fibronectin.

Target Information

Fibronectin is a disulfide-bonded dimer with a molecular weight range of 230-250 kDa. In the extracellular matrix of several connective tissues and vessels, fibronectin is present as an insoluble protein that is extensively cross-linked by interchain disulfide bonds forming high molecular mass polymers. Fibronectin is most abundant during embryonic development and tissue remodeling. Fibronectin is also present at high concentrations as a soluble plasma protein. Fibronectin is organized as a linear series of repeating modules which form domains for interaction with fibronectin itself, other matrix components (e.g. collagen and heparin) and receptors on cells (e.g. integrins). Fibronectin is present in a soluble dimeric form in plasma, and in a dimeric or multimeric form at the cell surface and in extracellular matrix. Fibronectin is involved in cell adhesion and migration processes including embryogenesis, wound healing, blood coagulation, host defense, and metastasis. Fibronectin has been implicated in carcinoma development in lung cancer. Further, Fibronectin expression is increased especially in non-small cell lung carcinoma. The adhesion of lung carcinoma cells to Fibronectin enhances tumorgenecity and confers resistance to apoptosis induced by standard chemotherapeutic agents. The gene encoding Fibronectin has three regions subject to alternative splicing, with the potential to produce 20 different transcript variants. However, the full-length nature of some Fibronectin variants has not been determined.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

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Bioinformatics

Protein Aliases: CIG; Cold insoluble globulin (CIG); Cold-insoluble globulin; DKFZp686F10164; DKFZp686H0342; DKFZp686I1370; DKFZp686O13149; ferritin L subunit; ferritin L-chain; Fibronectin; FN; Migration stimulating factor (MSF); migration-stimulating factor

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Gene Aliases: CIG; E330027I09; ED-B; FIBNEC; FINC; FN; Fn-1; FN1; FNZ; GFND; GFND2; LETS; MSF

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UniProt ID: (Human) P02751, (Mouse) P11276

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Entrez Gene ID: (Human) 2335, (Mouse) 14268, (Rat) 25661

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Function(s)
protease binding integrin binding protein binding collagen binding heparin binding peptidase activator activity identical protein binding mercury ion binding extracellular matrix structural constituent extracellular matrix structural protein extracellular matrix protein
Process(es)
angiogenesis cell activation regulation of protein phosphorylation platelet degranulation response to ischemia acute-phase response cell-substrate junction assembly cell adhesion calcium-independent cell-matrix adhesion positive regulation of cell proliferation glial cell migration regulation of cell shape response to wounding response to ozone positive regulation of gene expression positive regulation of peptidase activity peptide cross-linking extracellular matrix disassembly extracellular matrix organization integrin activation substrate adhesion-dependent cell spreading cellular response to vascular endothelial growth factor stimulus endodermal cell differentiation cellular response to platelet-derived growth factor stimulus wound healing negative regulation of apoptotic process positive regulation of axon extension positive regulation of fibroblast proliferation leukocyte migration positive regulation of chemotaxis response to glucocorticoid regulation of ERK1 and ERK2 cascade cellular response to lipopolysaccharide cellular response to mercury ion cellular response to glucose stimulus cellular response to interleukin-1 cellular response to prostaglandin E stimulus cellular response to transforming growth factor beta stimulus cellular response to BMP stimulus positive regulation of substrate-dependent cell migration, cell attachment to substrate negative regulation of transforming growth factor-beta secretion cell-matrix adhesion positive regulation of cell migration ossification
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