Recombinant human Fibronectin is produced in E. coli and supplied in a tag-free format, preserving the native sequence for versatile research use. While lacking eukaryotic glycosylation, this protein maintains key functional domains, making it suitable for studying extracellular matrix (ECM) biology, cell adhesion, and protein–protein interactions in a cost-effective manner.

Fibronectin is a high-molecular-weight ECM glycoprotein that plays a central role in cell adhesion, migration, and wound healing. It interacts with integrins and other ECM components to regulate processes such as angiogenesis, morphogenesis, and tissue remodeling. Recombinant fibronectin from E. coli provides a practical tool for biochemical assays, coating studies, and integrin-binding research where post-translational modifications are not required.