Recombinant Human Fibronectin Protein, CF

Product Discontinued

Recombinant Human Fibronectin Protein, CF Summary

• Details of Functionality: 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 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.
• Source: Mouse myeloma cell line, NS0-derived human Fibronectin protein
  Gln32-Pro1908, with a C-terminal 6-His tag
• Accession #: CAE45932
• N-terminal Sequence: No results obtained: Gln32 predicted
• Protein/Peptide Type: Recombinant Proteins
• Gene: FN1
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 206.6 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 190-210 kDa, reducing conditions

Packaging, Storage & Formulations

• 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.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS and Tween® 20.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Fibronectin Protein, CF

• CIG
• ED-B
• fibronectin 1
• Fibronectin
• FINC
• FN
• FN1
• FNZ
• GFND
• GFND2
• LETS
• MSF
• SMDCF

Background

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.

Publications for Fibronectin (4305-FN)(7)

Publications using 4305-FN

• T Bluhmki, S Traub, AK Müller, S Bitzer, E Schruf, MT Bammert, M Leist, F Gantner, JP Garnett, R Heilker Functional human iPSC-derived alveolar-like cells cultured in a miniaturized 96?Transwell air-liquid interface model Scientific Reports, 2021-08-23;11(1):17028. 2021-08-23 [PMID: 34426605] (Bioassay, Human)
• 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 Nonimmune cell-derived ICOS ligand functions as a renoprotective alphavbeta3 integrin-selective antagonist J. Clin. Invest., 2019-03-18;129(4):1713-1726. 2019-03-18 [PMID: 30747722] (Surface Plasmon Resonance (SPR, Human)
• C Frémin, JP Guégan, C Plutoni, J Mahaffey, MR Philips, G Emery, S Meloche ERK1/2-induced phosphorylation of R-Ras GTPases stimulates their oncogenic potential Oncogene, 2016-04-18;0(0):. 2016-04-18 [PMID: 27086924] (Bioassay, Human)
• Jeon M, Lee J, Nam S, Shin I, Lee J, Kim S Induction of fibronectin by HER2 overexpression triggers adhesion and invasion of breast cancer cells. Exp Cell Res, 2015-03-03;333(1):116-26. 2015-03-03 [PMID: 25743092] (Bioassay, Human)
• Ayala-Lujan , Jorge Lu, Vijayakumar , Vidhya, Gong , Mei, Smith , Rachel, Santiago , Araceli, Ruiz-Perez , Fernando Broad spectrum activity of a lectin-like bacterial serine protease family on human leukocytes. PLoS ONE, 2014-09-24;9(9):e107920. 2014-09-24 [PMID: 25251283] (Enzyme Assay, Enzyme Assay Substrate, Bacteria, Human)
• Dodd K, Yang J, Shen M, Sampson J, Tee A mTORC1 drives HIF-1alpha and VEGF-A signalling via multiple mechanisms involving 4E-BP1, S6K1 and STAT3. Oncogene, 2014-06-16;34(17):2239-50. 2014-06-16 [PMID: 24931163] (Bioassay, Human, Mouse)
• Chang , Mei-Ying, Huang , Duen-Yi, Ho , Feng-Min, Huang , Kuo-Chin, Lin , Wan-Wan PKC-dependent human monocyte adhesion requires AMPK and Syk activation. PLoS ONE, 2012-07-25;7(7):e40999. 2012-07-25 [PMID: 22848421] (Bioassay, Human)

Bioinformatics

• Gene Symbol: FN1
• Uniprot:
  • CAE45932()