CIG;ED-B;FINC;FN;FN1;FNZ;Fibronectin;GFND;GFND2;LETS;MSF

HEK293 Cells

Ser607-Pro1265

P02751

Human

72.4 kDa

90 kDa

C-His

Not validated for activity

> 95% as determined by reducing SDS-PAGE.

< 1.0 EU/mg of the protein as determined by the LAL method

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

This product is provided as lyophilized powder which is shipped with ice packs.

Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol.

It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.

Fibronectin (FN) is a glycoprotein component of the extracellular matrix of the extracellular matrix (ECM) with roles in embryogenesis, development, and wound healing. More recently, FN has emerged as player in platelet thrombus formation and diseases associated with thrombosis including vascular remodeling, atherosclerosis, and cardiac repair following a myocardial infarct. Each monomer of FN consists of three types of homologous repeating units, that is 12 type I repeats, two type II repeats and 15-17 type III repeats. 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. As an ECM component and one of the primary cell adhesion molecules, Fibronectin can be a ligand for fibrin, heparin, chondroitin sulfate, collagen/gelatin, as well as many integrin receptors through which FN mediates the variety of cellular signaling pathways. The study of solid human tumors showed among the early signs of malignant transformation the fragmentation of pericellular FN, concommitent with the increase of its production by the peritumoral stroma. These results should encourage further investigations concerning the potential importance of Fn production and breakdown during cancer progression. FN1 expression has been described to increase significantly from the morula towards the early blastocyst stage, suggesting that FN1 may also be involved in early blastocyst formation.