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Fibronectin is a multi-domain glycoprotein composed of an array of multiple repeated modular structures. Cellular fibronectin, an adhesion glycoprotein of the extracellular matrix, exists as a dimer with a molecular mass of ~ 550 kDa. This structure is composed of two heterodimers, the A chain and the B chain containing the type III connecting segment region. Cellular fibronectin differs from plasma fibronectin by the presence of additional polypeptide segments and its capacity to specifically regulate morphology and growth of attached cells including stem cells. Multiple domains of fibronectin show binding affinities for collagen, fibrin, heparin, and specific cell membrane receptors including integrins, as well as modulate cell adhesion. Fibronectin matrix assembly is essential for normal development and contributes to the generation of tumor metastases.