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F3542

Sigma-Aldrich

Fibronectin Fragment III1-C human

recombinant, expressed in E. coli, lyophilized powder

Sinonimo/i:

FF III1-C

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About This Item

Numero MDL:
MFCD00283226
Codice UNSPSC:
12352202
NACRES:
NA.75

Origine biologica

human

Livello qualitativo

200

Ricombinante

expressed in E. coli

Stato

lyophilized powder

Qualità

essentially salt free

PM

8-15 kDa

Confezionamento

pkg of 0.5 mg

tecniche

cell culture | mammalian: suitable

Copertura della superficie

0.45 μg/cm2

Solubilità

Tris-buffered saline: soluble 1.00-1.10 mg/mL, clear, colorless

N° accesso UniProt

P02751

Condizioni di spedizione

ambient

Temperatura di conservazione

−20°C

Informazioni sul gene

human ... FN1(2335)

Descrizione generale

Fibronectins are made of two subunits linked by disulfide bonds at the C terminal. In the extracellular matrix fibrils, fibronectins are further disulfide bonded into high molecular weight polymers. Fibronectin subunits vary in size between approximately 235 and 270 kD depending on tissue and species. Each subunit is made of repeating modules of three types: I, II, and III. There are 12 type I repeats, approximately 45 amino acids long, clustered in three groups, two adjacent type II repeats each 60 amino acids long, and 15-17 type III repeats each about 90 amino acids long. Type I and type II each contains two disulfide bonds, while type III lacks disulfide bonds. There are two free sulfhydryl groups per subunit at the type III repeat.

Recently a new region, type III1 repeat cloned from human placenta cDNA, was reported to participate in matrix formation. In an experiment employing antibodies for the analysisof fibronectin domains required for matrix assembly, the epitope that inhibited binding and insolubilization of labeled plasma fibronectin by fibroblasts, was identified on the type III1 and type I modules of fibronectin. This suggested a role for type III1 and type I in the mediation of fibronectin assembly. This finding was further supported by the ability of the 14 kDa fragment from the first two type III repeats of fibronectin to inhibit fibronectin matrix assembly.4 Recently recombinant fragment III1-C, modeled after the C-terminal two-thirds of the III1 repeat, was found to bind to fibronectin and induce spontaneous disulfide crosslinking of the fibronectin molecules into multimers, which resemble matrix fibrils

Applicazioni

Epithelial cells, mesenchymal cells, neuronal cells, fibroblasts, neural crest cells, endothelial cells

Azioni biochim/fisiol

Promotes cross-linking of fibronectin to form matrix fibril-like multimers.

Confezionamento

Package size based on protein content

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

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Certificati d'analisi (COA)

Lot/Batch Number
123M4108V
11131016
042M4080V
11110734
040M4104

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K C Ingham et al.
The Journal of biological chemistry, 272(3), 1718-1724 (1997-01-17)
The first type III module of fibronectin (Fn) contains a cryptic site that binds Fn and its N-terminal 29 kDa fragment and is thought to be important for fibril formation (Morla, A., Zhang, Z., and Ruoslahti, E. (1994) Nature 367
D C Hocking et al.
The Journal of biological chemistry, 269(29), 19183-19187 (1994-07-22)
Cultured fibroblasts express binding sites for the amino-terminal region of fibronectin on their cell surface that mediate the assembly of soluble fibronectin into disulfide-stabilized fibrils. These binding sites have been termed matrix assembly sites and have been studied in binding
A Morla et al.
Nature, 367(6459), 193-196 (1994-01-13)
Fibronectin is an extracellular matrix protein that is important in development, wound healing and tumorigenesis. In the blood it is dimeric, but in tissues forms disulphide crosslinked fibrils. Here we show that a fragment from the first type-III repeat of
Fatemeh Khodabandehloo et al.
Journal of cellular and molecular medicine, 25(11), 5138-5149 (2021-05-04)
Multipotent human bone marrow-derived mesenchymal stem cells (hMSCs) are promising candidates for bone and cartilage regeneration. Toll-like receptor 4 (TLR4) is expressed by hMSCs and is a receptor for both exogenous and endogenous danger signals. TLRs have been shown to
Mitsutaka Nishida et al.
Bioscience, biotechnology, and biochemistry, 78(4), 635-643 (2014-07-19)
Although previous reports have suggested that pectin induces morphological changes of the small intestine in vivo, the molecular mechanisms have not been elucidated. As heparan sulfate plays important roles in development of the small intestine, to verify the involvement of

Articoli

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Fibronectin (FN) is a multifunctional, extracellular plasma glycoprotein produced by hepatocytes that circulates at near micromolar concentration and assembles into extracellular matrix fibrils at cell surfaces along with locally produced cellular FN.

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Extracellular Matrix Proteins and Tools for Cell Culture Optimization

Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.

Protocolli

Fibronectin Coating Protocol

Dilute fibronectin to the desired concentration. Optimum conditions for attachment are dependent on cell type and application. The typical coating concentration is 1 – 5 ug/cm2.Fibronectin coating protocol, products, and FAQs at sigmaaldrich.com

Fibronectin Coating Protocol

Dilute fibronectin to the desired concentration. Optimum conditions for attachment are dependent on cell type and application. The typical coating concentration is 1 – 5 ug/cm2.Fibronectin coating protocol, products, and FAQs.

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