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F3542

Sigma-Aldrich

Fibronectin Fragment III1-C human

recombinant, expressed in E. coli, lyophilized powder

Synonym(e):

FF III1-C

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352202
NACRES:
NA.75

Biologische Quelle

human

Qualitätsniveau

Rekombinant

expressed in E. coli

Form

lyophilized powder

Qualität

essentially salt free

Mol-Gew.

8-15 kDa

Verpackung

pkg of 0.5 mg

Methode(n)

cell culture | mammalian: suitable

Oberflächendeckung

0.45 μg/cm2

Löslichkeit

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

UniProt-Hinterlegungsnummer

Versandbedingung

ambient

Lagertemp.

−20°C

Angaben zum Gen

human ... FN1(2335)

Allgemeine Beschreibung

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

Anwendung

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

Biochem./physiol. Wirkung

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

Verpackung

Package size based on protein content

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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

Artikel

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.

Cancer stem cell media, spheroid plates and cancer stem cell markers to culture and characterize CSC populations.

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

Protokolle

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

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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