Fibronectin

Cellular fibronectin is an adhesion glycoprotein of theextracellular matrix, which exists as a dimer with a molecular mass of ~550 kDa. It contains two heterodimers, the A chain and the B chain containing the type III connecting segment (IIIcs) region. Cellular fibronectin differs from plasma fibronectin, a 200–250 kDa monomer, by the presence of additional polypeptide segments and in altering morphology of transformed cells and hemagglutination. Different forms of fibronectin appear to be generated from tissue specific splicing of fibronectin mRNA, transcribed from a single gene. Multiple domains of fibronectin show binding affinities for collagen, fibrin, heparin, and specific cell membrane receptors. The most notable domain, Arg-Gly-Asp (RGD), is recognized by integrins and mediates cell adhesion. Fibronectin is involved in widespread interactions and functions, such as the attachment and migration of many cell types, cytoskeletal assembly, tyrosine phosphorylation, and metastasis. 

Fibronectin Products

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