Fibronectin is an attachment factor that facilitates the attachment and cytoplasmic spreading of all types of anchorage-dependent cells. It is responsible for cell adhesion and migration processes including embryogenesis, wound healing, blood coagulation, host defense, and metastasis. Fibronectin is a cell surface-associated glycoprotein, high molecular weight, soluble, disulfide-linked dimer. It is an extracellular matrix (ECM) protein found in abundance in blood, connective tissues and other provisional matrices while demonstrating functions in both cell-to- cell and cell-to-matrix interactions. Fibronectin functions not only as a general cell adhesion molecule but also as a modulator by binding between cell surfaces and the ECM via a central cell-binding domain known simply as RGD (Arg-Gly-Asp). It appears that the RGD domain serves to activate and align the Fibronectin interface and a synergy site provides the mechanical strength to the bond. Fibronectin is particularly useful for the culture of cells that are not capable of synthesizing their own biomatrix or when culturing cells in serum-free medium. It is a clear sterile solution containing fibronectin obtained by affinity purification on gelatin-sepharose from bovine plasma. This solution contains buffer salts. Normal attachment, growth and development of many cell types are dependent on attachment factors and extracellular matrix (ECM) components.
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