Are you struggling with prolonged drug development cycles or inconsistent outcomes in fibrosis or oncology research? Creative Biolabs' fibronectin specific Neutra™ antibody products leverage advanced hybridoma screening and epitope-specific engineering to deliver high-affinity, rigorously validated antibodies that accelerate target validation and therapeutic candidate optimization.
Fibronectin, a high-molecular-weight glycoprotein, serves as a key mediator of cell adhesion, migration, and extracellular matrix (ECM) organization. It exists in three primary isoforms: plasma-derived (synthesized by hepatocytes), cellular (secreted by fibroblasts), and fetal (abundant in placental tissues). This multifunctional protein dynamically interacts with integrin receptors and ECM components, bridging mechanical and biochemical signaling across tissues.
Fibronectin comprises two nearly identical subunits linked by disulfide bonds at their C-termini. Each subunit (~220–250 kDa) contains repeating modules—type I, II, and III domains—that mediate binding to collagen, heparin, and cell-surface integrins. The Arg-Gly-Asp (RGD) motif within the III10 domain is critical for integrin α5β1 recognition, enabling cellular adhesion. Cryo-EM studies reveal conformational flexibility in Fibronectin fibrils, which adapt to mechanical stress during ECM remodeling.
Fibronectin-integrin binding activates intracellular pathways including MAPK, PI3K/AKT, and FAK/Src, regulating cell proliferation, survival, and differentiation. Crosstalk with growth factor receptors (e.g., TGF-β) amplifies profibrotic signaling in pathological ECM deposition. Conversely, Fibronectin degradation by matrix metalloproteinases (MMPs) releases bioactive fragments that modulate angiogenesis and inflammation.
Fig.1 The schematic diagram for how fibronectin functions in glioma stem-like cells (GSCs).1
Aberrant Fibronectin expression correlates with liver cirrhosis, pulmonary fibrosis, and tumor metastasis. Elevated plasma Fibronectin levels signal active fibrogenesis, while reduced levels indicate hepatic dysfunction. In cancer, Fibronectin-rich ECM fosters metastatic niche formation by enhancing tumor cell invasiveness and chemoresistance.
Plasma Fibronectin quantification using ELISA or lateral flow assays enables non-invasive monitoring of liver fibrosis progression and therapeutic response in clinical trials.
Neutralizing antibodies targeting Fibronectin-integrin interactions reduce collagen deposition in preclinical models of pulmonary fibrosis, offering a pathway for combination therapies with antifibrotic small molecules.
Inhibition of Fibronectin-mediated cancer cell adhesion impedes metastasis in murine xenograft models. Antibodies conjugated to imaging agents improve intraoperative visualization of tumor margins.
Fibronectin-coated scaffolds enhance stem cell engraftment and differentiation in regenerative medicine applications, achieving 95% cell viability in 3D bioprinting workflows.
Creative Biolabs' anti-Fibronectin antibodies are engineered for specificity to functional domains (e.g., RGD, heparin-binding regions) and validated across applications:
- Neutralizing Antibodies: Block integrin binding to disrupt fibrotic signaling or tumor cell adhesion.
- Diagnostic Antibodies: Quantify plasma Fibronectin for early detection of liver fibrosis (sensitivity: 92%; specificity: 88%).
- Functional Assay Tools: Monitor ECM remodeling dynamics via immunofluorescence or traction force microscopy.
Rigorous lot-to-lot consistency ensures reproducibility in preclinical models, supporting IND-enabling studies.
Creative Biolabs' fibronectin specific Neutra™ antibody products equip researchers with tools to overcome ECM-related challenges in drug discovery and diagnostics.
Contact our scientific team today to discuss custom solutions for your project.
Recombinant Anti-Fibronectin Antibody (V3S-0522-YC6201) (CAT#: V3S-0522-YC6201)
Target: Fibronectin
Host Species: Mouse
Application: WB,