Invitrogen™ Fibronectin Monoclonal Antibody (A17)

Description

CSI 005-17-02 is highly specific for fibronectin. There is no evidence for cross-reactivity with other connective tissue proteins (vitronectin, elastin, collagen, laminin). CSI 005-17-02 cross-reacts with human and chicken fibronectin. Other species have not been tested. CSI 005-17-02 has been successfully used in Western blottin, ELISA, Immunohistochemistry and Immunoprecipitation procedures. The antibody inhibits integrin-mediated cell adhesion to the cell binding domain of fibronectin. It can be used to probe fibronectin conformation. Strong reaction is seen in ELISA with thrombospondin directly coated onto the microtiter well. The specificity of the CSI 005-17-02 epitope is located in the 120 kDa cell binding fragment. 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.