Human Fibronectin

General description
Fibronectin (FN) is a glycoprotein with 5-9% carbohydrates present as N- and O-linked oligosaccharides.[1] It belongs to the ligand glycoprotein family. The FN gene is localized to human chromosome 2q35.[2] FN exists as two major isoforms, plasma-based soluble and extracellular matrix (ECM)-based insoluble form.[1] Fibronectin structure comprises repeats of FNI, FNII and FNIII repeats.[3] It also has fibrin-binding sites and exists as a dimer.[4] Alternative splicing of the FN1 gene leads to the generation of many isoforms.[1] This fibronectin protein is manufactured in human cells using an all-human production system with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports better stability of the protein in culture.
Application
Epithelial cells, mesenchymal cells, neuronal cells, fibroblasts, neural crest cells, endothelial cells.
Recommended for use as a cell culture substratum at 1-5 μg/cm2 or 0.5-50 μg/ml. Optimal concentration depends on cell type as well as the application or research objectives.
Fibronectin human has been used for coating cell culture plates for culturing endothelial progenitor cells.[5] It has also been used as a component of Dulbecco′s modified Eagle′s medium (DMEM) in the in vitro matrigel invasion assay of glioblastoma cells.[6] Biochem/physiol Actions
Fibronectin (FN) is essential for embryonic development and mediates cell adhesion and migration functions.[2] It mediates apoptosis in nasopharyngeal carcinoma (NPC). The plasma FN regulates thrombosis.[1] Fibronectin functions as a ligand for the integrin receptor family[4] and contains collagen, glycoprotein and glycosaminoglycan binding sites.[7] Mutation in the FNI gene leads to an imbalance in the soluble and insoluble forms of fibronectin leading to glomerular deposits in hereditary kidney disease, glomerulopathy.[8] Missense mutations in the FN1 gene are implicated in the skeletal dysplasias disorder, Spondylometaphyseal dysplasias.[7] Features and Benefits
Human-derived fibronectin
Produced through recombinant expression in HEK 293 cells
Low endotoxin levels
Absence of bacterial contamination
Physical form
Supplied as a powder, lyophilized from CAPS buffered saline.
Analysis Note
The biological activity of recombinant human fibronectin was tested in culture by measuring the ability of immobilized fibronectin to support adhesion of CHO cells.