Fibronectina

Fibronectin proteolytic fragment from human plasma has been used as fluorophore-conjugated proteins. It has also been used in solid phase binding assay.

Fibronectin participates in cell adhesion, growth, migration, wound healing, blood coagulation and metastasis. Mutations in FN1 results in glomerulopathy. It plays an important role in cell attachment and spreading, control of cell cytoskeleton, morphology and differentiation. FN1 is also involved in extracellular matrix formation, hemostasis and thrombosis. Proteolytic fragments of fibronectin plays a vital role in mononuclear phagocyte function.

Fibronectins are high molecular weight glycoproteins with two subunits joined by a disulfide bond to form the dimer. The fragments are obtained using protelytic enzymes. This 45 kDa gelatin binding fragment is obtained through trypitc digestion of the N-terminal 70 kDa fragment, which is produced by Cathespin D digestion.

This fragment has an acidic pI (4.9-5.3) and does not bind to heparin. This domain is resistant to proteolysis due to intrachain disulfide bonding and the attached carbohydrate. The intrachain disulfide bonds are essential for binding to gelatin, while the complex, branched, asparagine-linked carbohydrate is not. This fragment binds to C1q, but not to fibrin.

The product should be stored at -20°C.

Fibronectin 1 is a glycoprotein of the extracellular matrix that is coded by FN1 gene. It is expressed in the plasma and at the cell surface.FN1 is mapped to human chromosome 2q35. Proteolytic fragments of fibronectin has a cell binding domain. Plasma fibronectin has two polypeptide chains connected by two disulphide bonds present near carboxy terminal. Each polypeptide chain is of 220-250 kDa.

This product is lyophilized from phosphate buffered saline with sucrose as a cryoprotectant. The source material has tested negative for antibody to HIV, HCN, and HBsAg. It is soluble in water at 0.5 mg/mL and yields a clear to slightly hazy solution.