Measured by the ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. When cells are added to Fibronectin coated plates (2.5 μg/mL and 100 μL/well), approximately 35%-60% cells will adhere specifically after 35 minutes at 37℃.

Fibronectin Protein, Human, Recombinant (aa 607-1265, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 73.2 kDa and the accession number is P02751-15.

Human

HEK293 Cells

GFND,LETS,ED-B,fibronectin 1,CIG,GFND2,FNZ,FINC,FN,MSF

Fragment 2 (Ser607-Pro1265) of Human Fibronectin (NP_997647.1)

≥ 97 % as determined by SDS-PAGE. ≥ 95 % as determined by SEC-HPLC.

A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.

It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

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. The fragment 2 of FN comprises the first 7 FN type III repeats and is suggested to be important for self association during fibril growth via the key module III2.