Fibronectin Protein, Human (Biotinylated, His-Avi)

Fibronectin, a versatile glycoprotein, plays a crucial role in cellular interactions by binding to various compounds such as collagen, fibrin, heparin, DNA, and actin. Its involvement in cell adhesion, motility, opsonization, wound healing, and maintenance of cell shape underscores its significance in fundamental cellular processes. Fibronectin also contributes to osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization, and regulates the deposition of type I collagen by osteoblasts. Acting as a ligand for the LILRB4 receptor, Fibronectin inhibits FCGR1A/CD64-mediated monocyte activation. Moreover, Fibronectin's ability to induce fibril formation, as observed in the fibronectin polymer named superfibronectin, imparts enhanced adhesive properties. Notably, both anastellin and superfibronectin exhibit inhibitory effects on tumor growth, angiogenesis, and metastasis, with anastellin activating p38 MAPK and inhibiting lysophospholipid signaling. The multifaceted functions of Fibronectin underscore its pivotal role in cellular dynamics and its potential as a target for therapeutic interventions in various pathological conditions.