Recombinant Human Fibronectin Protein, CF Summary
Product Specifications
Fibronectin can also be added to the media to support cell spreading at a concentration of 0.5-50 μg/mL.
Gln32-Pro1908, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
4305-FN
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS and Tween® 20. |
Reconstitution | Reconstitute at 100 μg/mL in sterile 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.
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Reconstitution Calculator
Background: Fibronectin
Fibronectin (FN) is a large, modular glycoprotein that generates a polymeric fibrillar network in the extracellular matrix (ECM), and forms 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 fibrillar network. 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 its sensitivity to proteases (6, 7). The tilt angle between type III domains #9 and #10 (which contains an RGD motif) determines integrin binding affinity, suggesting how structural differences between fibrillar and soluble Fibronectin may influence their function (8). From the N-terminus to the furin cleavage site at amino acid 1908, human Fibronectin shares 92% amino acid sequence identity with mouse and rat Fibronectin.
- Mao, Y. and J.E. Schwarzbauer (2005) Matrix Biol. 24:389.
- Potts, J.R. and I.D. Campbell (1996) Matrix Biol. 15:313.
- Bernard, M.P. et al. (1985) Biochemistry 24:2698.
- Kornblihtt, A.R. et al. (1983) Proc. Natl. Acad. Sci. USA 80:3218.
- Kornblihtt, A.R. et al. (1985) EMBO J. 4:1755.
- Mould, A.P. et al. (1991) J. Biol. Chem. 266:3579.
- Abe, Y. et al. (2005) Biochem. Biophys. Res. Commun. 338:1640.
- Altroff, H. et al. (2004) J. Biol. Chem. 279:55995.
Citations for Recombinant Human Fibronectin Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 7
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Functional human iPSC-derived alveolar-like cells cultured in a miniaturized 96?Transwell air-liquid interface model
Authors: T Bluhmki, S Traub, AK Müller, S Bitzer, E Schruf, MT Bammert, M Leist, F Gantner, JP Garnett, R Heilker
Scientific Reports, 2021-08-23;11(1):17028.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Nonimmune cell-derived ICOS ligand functions as a renoprotective alphavbeta3 integrin-selective antagonist
Authors: KH Koh, Y Cao, S Mangos, NJ Tardi, RR Dande, HW Lee, B Samelko, MM Altintas, VP Schmitz, H Lee, K Mukherjee, V Peev, DJ Cimbaluk, J Reiser, E Hahm
J. Clin. Invest., 2019-03-18;129(4):1713-1726.
Species: Human
Sample Types: Recombinant Protein
Applications: Surface Plasmon Resonance (SPR -
ERK1/2-induced phosphorylation of R-Ras GTPases stimulates their oncogenic potential
Authors: C Frémin, JP Guégan, C Plutoni, J Mahaffey, MR Philips, G Emery, S Meloche
Oncogene, 2016-04-18;0(0):.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Induction of fibronectin by HER2 overexpression triggers adhesion and invasion of breast cancer cells.
Authors: Jeon M, Lee J, Nam S, Shin I, Lee J, Kim S
Exp Cell Res, 2015-03-03;333(1):116-26.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Broad spectrum activity of a lectin-like bacterial serine protease family on human leukocytes.
Authors: Ayala-Lujan, Jorge Lu, Vijayakumar, Vidhya, Gong, Mei, Smith, Rachel, Santiago, Araceli, Ruiz-Perez, Fernando
PLoS ONE, 2014-09-24;9(9):e107920.
Species: Bacteria, Human
Sample Types: Protein, Whole Cells
Applications: Enzyme Assay, Enzyme Assay Substrate -
mTORC1 drives HIF-1alpha and VEGF-A signalling via multiple mechanisms involving 4E-BP1, S6K1 and STAT3.
Authors: Dodd K, Yang J, Shen M, Sampson J, Tee A
Oncogene, 2014-06-16;34(17):2239-50.
Species: Human, Mouse
Sample Types: Whole Cells
Applications: Bioassay -
PKC-dependent human monocyte adhesion requires AMPK and Syk activation.
Authors: Chang, Mei-Ying, Huang, Duen-Yi, Ho, Feng-Min, Huang, Kuo-Chin, Lin, Wan-Wan
PLoS ONE, 2012-07-25;7(7):e40999.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
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