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F3542

Sigma-Aldrich

Fibronectin Fragment III1-C human

recombinant, expressed in E. coli, lyophilized powder

Synonim(y):

FF III1-C

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About This Item

Numer MDL:
MFCD00283226
Kod UNSPSC:
12352202
NACRES:
NA.75

pochodzenie biologiczne

human

Poziom jakości

200

rekombinowane

expressed in E. coli

Postać

lyophilized powder

jakość

essentially salt free

masa cząsteczkowa

8-15 kDa

opakowanie

pkg of 0.5 mg

metody

cell culture | mammalian: suitable

pokrycie powierzchni

0.45 μg/cm2

rozpuszczalność

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

numer dostępu UniProt

P02751

Warunki transportu

ambient

temp. przechowywania

−20°C

informacje o genach

human ... FN1(2335)

Powiązane kategorie

Opis ogólny

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

Zastosowanie

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

Działania biochem./fizjol.

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

Opakowanie

Package size based on protein content

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)

Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
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
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

Produkty

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Fibronektyna

Fibronektyna (FN) odgrywa kluczową rolę w tworzeniu fibryli macierzy zewnątrzkomórkowej i interakcjach komórkowych.

Cancer Stem Cells: Targets for Cancer Therapy

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

Protokoły

Fibronectin Coating Protocol

Dilute fibronectin for cell attachment, varying per cell type. Coating protocol, products, and FAQs provided.

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