F3542
Fibronectin Fragment III1-C human
recombinant, expressed in E. coli, lyophilized powder
Synonym(s):
FF III1-C
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About This Item
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biological source
human
Quality Level
recombinant
expressed in E. coli
form
lyophilized powder
quality
essentially salt free
mol wt
8-15 kDa
packaging
pkg of 0.5 mg
technique(s)
cell culture | mammalian: suitable
surface coverage
0.45 μg/cm2
solubility
Tris-buffered saline: soluble 1.00-1.10 mg/mL, clear, colorless
UniProt accession no.
shipped in
ambient
storage temp.
−20°C
Gene Information
human ... FN1(2335)
General description
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
Biochem/physiol Actions
Promotes cross-linking of fibronectin to form matrix fibril-like multimers.
Packaging
Package size based on protein content
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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)
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