Fibronectin also known as FN is a high-molecular-weight glycoprotein discovered abroad in 1974. As one of the primary cell adhesion molecules FN plays a crucial role in numerous vital physiological processes such as embryogenesis wound healing hemostasis and thrombosis. Altered expression degradation and assembly of FN are closely associated with numerous pathological conditions including cancer and fibrosis. As a biochemical reagent it provides a foundation for industrial applications in cell culture and bioengineering. Among FN’s many functions the most fundamental and critical is promoting cell adhesion and growth. Cell adhesion is essential for maintaining bodily structure and completing cellular growth. Recombinant human fibronectin comprises three functional domains: the cell-binding domain the high-affinity heparin-binding domain and the CS1 site. This product is manufactured through fermentation separation and high-purity filtration from a yeast expression system containing a highly efficient fibronectin gene. It consists of a polypeptide chain of 574 amino acid residues with a molecular weight of 63 kDa.