Biotinylated Recombinant Human Fibronectin ED-B (N-His&Avi)
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| Amount : | 50 µg |
| Content : | Supplied as a 0.2 um filtered solution of 50mM Tris, 150mM NaCl, pH7.2. |
| AA sequence : | Recombinant Human Fibronectin is produced by our E.coli expression system and the target gene encoding Glu5-Thr95 is expressed with a 6His, Avi tag at the N-terminus. |
| Alternative Name : | Fibronectin; FN1 |
Source : E. coli;
Fibronectin is a high-molecular-weight glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. Similar to integrins, fibronectin binds extracellular matrix components such as collagen, fibrin, and heparan sulfate proteoglycans. The occurrence of multiple isoforms results from alternative mRNA splicing of the ED-A, ED-B and III-CS regions, and subsequent post-translational modification. Fibronectin plays a critical role in cell adhesion, growth, migration, and differentiation, and it is important for the processes of wound healing and embryonic development. Altered fibronectin expression, degradation, and organization has been associated with a number of pathologies, including cancer and fibrosis. Studies of solid human tumors showed among the early signs of malignant transformation the fragmentation of pericellular fibronectin, concomitant with the increase of its production by the peritumoral stroma. These results have encouraged further investigations of the potential importance of fibronectin production and breakdown during cancer progression.
Fibronectin is a high-molecular-weight glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. Similar to integrins, fibronectin binds extracellular matrix components such as collagen, fibrin, and heparan sulfate proteoglycans. The occurrence of multiple isoforms results from alternative mRNA splicing of the ED-A, ED-B and III-CS regions, and subsequent post-translational modification. Fibronectin plays a critical role in cell adhesion, growth, migration, and differentiation, and it is important for the processes of wound healing and embryonic development. Altered fibronectin expression, degradation, and organization has been associated with a number of pathologies, including cancer and fibrosis. Studies of solid human tumors showed among the early signs of malignant transformation the fragmentation of pericellular fibronectin, concomitant with the increase of its production by the peritumoral stroma. These results have encouraged further investigations of the potential importance of fibronectin production and breakdown during cancer progression.
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