|Recombinant Human Fibronectin Fragment 2 protein (Catalog#10314-H08H)|
|0.2 μm filtered solution in PBS with 5% trehalose|
|This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human Fibronectin Fragment 2 (Catalog#10314-H08H; Ser 607-Pro 1265; CAD91166). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.|
|Human Fibronectin Fragment 2
No cross-reactivity with Human cell lysate (293 cell line) in WB and ELISA.
ELISA: 0.5-1 μg/mL
This antibody can be used at 0.5-1 μg/mL with the appropriate secondary reagents to detect Fibronectin Fragment 2. The detection limit for Fibronectin Fragment 2 is approximately 0.16ng/well.
|This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free.|
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
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.