Recombinant Human Fibronectin Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Product Details
Citations (7)

Recombinant Human Fibronectin Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its ability to support cell attachment and spreading when used as a substratum for cell culture. In this application, the recommended concentration for this effect is typically 1-5 μg/cm2.
Fibronectin can also be added to the media to support cell spreading at a concentration of 0.5-50 μg/mL.
Optimal concentrations will need to be determined for individual user applications.
Mouse myeloma cell line, NS0-derived human Fibronectin protein
Gln32-Pro1908, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Gln32 (partially blocked)
Predicted Molecular Mass
207 kDa
200-250 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

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.

What formulation is right for me?

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 HEPES, NaCl and Tween®.
Reconstitution Reconstitute at 100 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.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
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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.

  1. Mao, Y. and J.E. Schwarzbauer (2005) Matrix Biol. 24:389.
  2. Potts, J.R. and  I.D. Campbell (1996) Matrix Biol. 15:313.
  3. Bernard, M.P. et al. (1985) Biochemistry 24:2698.
  4. Kornblihtt, A.R. et al. (1983) Proc. Natl. Acad. Sci. USA 80:3218.
  5. Kornblihtt, A.R. et al. (1985) EMBO J. 4:1755.
  6. Mould, A.P. et al. (1991) J. Biol. Chem. 266:3579.
  7. Abe, Y. et al. (2005) Biochem. Biophys. Res. Commun. 338:1640.
  8. Altroff, H. et al. (2004) J. Biol. Chem. 279:55995.
Entrez Gene IDs
2335 (Human); 280794 (Bovine)
Alternate Names
CIG; ED-B; fibronectin 1; Fibronectin; FINC; FN; FN1; FNZ; GFND; GFND2; LETS; MSF; SMDCF

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.

7 Citations: Showing 1 - 7
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  1. 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;11(1):17028.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. 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;129(4):1713-1726.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance (SPR
  3. 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;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. 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;333(1):116-26.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. 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, 2015;34(17):2239-50.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. 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;9(9):e107920.
    Species: Bacteria
    Sample Types: Protein
    Applications: Enzyme Assay Substrate
  7. 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;7(7):e40999.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay


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