F3542
Fibronectin Fragment III1-C human
recombinant, expressed in E. coli, lyophilized powder
Synonyme(s) :
FF III1-C
Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme
About This Item
Produits recommandés
Source biologique
human
Niveau de qualité
Produit recombinant
expressed in E. coli
Forme
lyophilized powder
Qualité
essentially salt free
Poids mol.
8-15 kDa
Conditionnement
pkg of 0.5 mg
Technique(s)
cell culture | mammalian: suitable
Couverture de surface
0.45 μg/cm2
Solubilité
Tris-buffered saline: soluble 1.00-1.10 mg/mL, clear, colorless
Numéro d'accès UniProt
Conditions d'expédition
ambient
Température de stockage
−20°C
Informations sur le gène
human ... FN1(2335)
Description générale
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
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
Application
Epithelial cells, mesenchymal cells, neuronal cells, fibroblasts, neural crest cells, endothelial cells
Actions biochimiques/physiologiques
Promotes cross-linking of fibronectin to form matrix fibril-like multimers.
Conditionnement
Package size based on protein content
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
Déjà en possession de ce produit ?
Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Les clients ont également consulté
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
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
Contacter notre Service technique