Recombinant Human Fibronectin/Anastellin Protein, CF Summary
Asn631-Pro705, with an N-terminal Met and a C-terminal 6-His tag
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 250 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Fibronectin (FN) is a large modular glycoprotein that is found as a polymeric fibrillar network in the extracellular matrix (ECM) and as soluble disulfide-linked dimeric protomers in plasma and other body fluids (1, 2). Fibronectin is a ligand for many molecules including fibrin, heparin, chondroitin sulfate, collagen/gelatin, and integrins. It is involved in multiple cellular processes such as cell adhesion/migration, blood clotting, morphogenesis, tissue repair, and cell signaling. Fibronectin functions are mediated by the insoluble polymeric fibrils. Conversion of soluble fibronectin to fibronectin fibrils in the ECM is initiated by binding to cell surface integrins, resulting in exposure of cryptic epitopes necessary for polymerization (1). Fibronectin is made up of three types of homologous structural motifs termed FN type I, type II, and type III repeats (3-5). Alternative splicing generates multiple isoforms of fibronectin which may have insertions of extra type III domains (EDA and EDB) or alteration of the type III connecting segment (IIICS) (5). Differential splicing within the IIICS domain determines the presence of CS1 and CS2 sequences and the sensitivity to proteases (6, 7). A fragment from the first type III repeat, known as Anastellin, binds to fibronectin and induces the formation of high molecular weight disulfide-linked superfibronectin (sFN) (8-10). sFN exhibits increased protease sensitivity and cellular adhesiveness compared to fibronectin (8, 10). Anastellin acts in vivo to inhbit angiogenesis, tumor growth, and metastasis (9).
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- Kornblihtt, A.R. et al. (1985) EMBO J. 4:1755.
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- Abe, Y. et al. (2005) Biochem. Biophys. Res. Commun. 338:1640.
- Morla, A. et al. (1994) Nature 367:193.
- Yi, M. and E. Rouslahti (2001) Proc. Natl. Acad. Sci. USA 98:620.
- Ohashi, T. and H.P. Erickson (2005) J. Biol. Chem. 280:39143.
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