Recombinant Human Fibronectin Fragment 3 Protein, CF

Catalog # Availability Size / Price Qty
3938-FN-050
R&D Systems Recombinant Proteins and Enzymes
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Citations (2)
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Recombinant Human Fibronectin Fragment 3 Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured by the ability of the immobilized protein to support the adhesion of B16‑F1 mouse melanoma cells. When 5 x 104 cells/well are added to Recombinant Human Fibronectin Fragment 3/amino acids
1266-1908 coated plates (1 µg/mL with 100 µL/well), approximately 50‑75% will adhere after 30-60 minutes at 37 °C.
Optimal concentration depends on cell type as well as the application or research objective.
Source
Mouse myeloma cell line, NS0-derived human Fibronectin protein
Glu1266-Pro1908 (Met1874Thr), with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Glu1266
Predicted Molecular Mass
70.1 kDa
SDS-PAGE
80-90 kDa, reducing conditions

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3938-FN

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.

3938-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.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: Fibronectin

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). The protein subunit 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). 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 in the ECM. 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). FN1.3 includes the EDB plus type III domains #8 - 13 and the initial region of domain 14. These domains facilitate association with heparin, myocilin, ApoA, and integrins alpha 5 beta 1 and alpha V beta 3 (6 - 10). The tilt angle between type III domains #9 and #10 (which contains an RGD motif) determines the affinity of interaction with these integrins, suggesting how structural differences between fibrillar and soluble Fibronectin may influence their function (10). Within FN1.3, human Fibronectin shares 97% and 92% aa sequence identity with mouse and rat Fibronectin, respectively.

References
  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. Peters, D.M. et al. (2005) Exp. Cell Res. 303:218.
  7. Edelstein, C. et al. (2005) J. Lipid Res. 46:2673.
  8. Pytela, R. et al. (1985) Cell 40:191.
  9. Wayner, E.A. et al. (1989) J. Cell Biol. 109:1321.
  10. 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 Fragment 3 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.

2 Citations: Showing 1 - 2
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  1. Probing fibronectin adsorption on chemically defined surfaces by means of single molecule force microscopy
    Authors: E Liamas, RA Black, PA Mulheran, R Tampé, R Wieneke, ORT Thomas, ZJ Zhang
    Scientific Reports, 2020;10(1):15662.
    Species: N/A
    Sample Types: Reference Standard
  2. Curli mediate bacterial adhesion to fibronectin via tensile multiple bonds
    Sci Rep, 2016;6(0):33909.
    Species: Bacteria
    Sample Types: Whole Cells
    Applications: Bioassay

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