Fibronectin Monoclonal Antibody (A32), Invitrogen™

Description

• CSI 005-32-02 is highly specific for fibronectin
• There is no evidence for cross-reactivity with other connective tissue proteins (vitronectin, elastin, collagen, laminin)
• CSI 005-32-02 cross-reacts with human fibronectin
• Other species have not been tested
• CSI 005-32-02 has been successfully used in Western blotting, ELISA, Immunohistochemistry and Immunoprecipitation procedures
• The antibody inhibits cell adhesion to fibronectin mediated by the heparin-binding domain
• It can be used to probe fibronectin conformation and to quantitate plasma fibronectin in a sandwich ELISA
• NOTE: Concentration is lot-dependent and can vary from 0.85-1.15 mg/mL Fibronectin is a disulfide-bonded dimer with a molecular weight range of 230-250 kDa
• In the extracellular matrix of several connective tissues and vessels, fibronectin is present as an insoluble protein that is extensively cross-linked by interchain disulfide bonds forming high molecular mass polymers
• Fibronectin is most abundant during embryonic development and tissue remodeling
• Fibronectin is also present at high concentrations as a soluble plasma protein
• Fibronectin is organized as a linear series of repeating modules which form domains for interaction with fibronectin itself, other matrix components (e.g
• collagen and heparin) and receptors on cells (e.g
• integrins)
• Fibronectin is present in a soluble dimeric form in plasma, and in a dimeric or multimeric form at the cell surface and in extracellular matrix
• Fibronectin is involved in cell adhesion and migration processes including embryogenesis, wound healing, blood coagulation, host defense, and metastasis
• Fibronectin has been implicated in carcinoma development in lung cancer
• Further, Fibronectin expression is increased especially in non-small cell lung carcinoma
• The adhesion of lung carcinoma cells to Fibronectin enhances tumorgenecity and confers resistance to apoptosis induced by standard chemotherapeutic agents
• The gene encoding Fibronectin has three regions subject to alternative splicing, with the potential to produce 20 different transcript variants
• However, the full-length nature of some Fibronectin variants has not been determined.