All kit components of this kit are stable at 2 to 8°C. Any unused reconstituted standard should be discarded or frozen at -70°C. Standard can be frozen and thawed one time only without loss of immunoreactivity.
< 0.910 ng/ml
Sample Type :
Human serum, plasma, cell lysate, cultuer supernatant, buffered solution
Fibronectin (FN) exists in two main forms: 1) as a soluble glycoprotein in blood plasma (plasma FN), and 2) as an insoluble glycoprotein in tissue extracellular matrices (cellular FN). Many different cell types synthesize fibronectin and secrete it as a disulfide-bonded dimer composed of 230–270 kDa subunits. FN is one of the largest multi-domain proteins that interact with a variety of macromolecules like heparin, collagen /gelatin, and fibrin. FN is involved in many cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/ adhesion and so can be used as a therapeutic agent for wound healing. In addition, its age-dependent increase in plasma and tissues may be accompanied in pathological states, especially in tumor growth, by its proteolytic breakdown.
Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.