Recombinant Human Fibronectin Fragment 4 Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Fibronectin Fragment 4 Protein, CF Summary

• Details of Functionality: Measured by the ability of the immobilized protein to support the adhesion of B16‑F1 mouse melanoma cells. The ED₅₀ for this effect is 0.05-0.35 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived human Fibronectin protein
  Val1913-Glu2477, with a C-terminal 6-His tag
• Accession #: NP_997647
• N-terminal Sequence: Val1913
• Protein/Peptide Type: Recombinant Proteins
• Gene: FN1
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 63.5 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: 70-95 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.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• 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 Fragment 4 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 is found in a polymeric fibrillar network in the extracellular matrix (ECM). It also forms a 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 fibrin, heparin, chondroitin sulfate, collagen/gelatin, and integrins. It is involved in multiple cellular processes including 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). FN1.4 contains one type III domain, the IIICS domain, three type I domains, and the site of interchain disulfide linkage. Within FN1.4, human fibronectin shares 91% and 88% aa sequence identity with mouse and rat fibronectin, respectively. FN1.4 contains regions that enable association with heparin and fibrin. The IIICS domain contains two sites (CS1 and CS2) that interact with integrin alpha 4 beta 1 (6-8). The CS1 sequence is not accessible in full length fibronectin but is exposed by protease digestion, thereby enabling cell adhesion via integrin alpha 4 beta 1 (9). This is distinct from integrin alpha 5 beta 1-mediated adhesion through an RGD motif located N-terminal to FN1.4 (10). Differential splicing within the IIICS domain determines the presence of CS1 and CS2 sequences and the sensitivity to proteases (6,11).

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. 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. Komoriya, A., et al. (1991) J. Biol. Chem. 266:15075.
8. Wayner, E.A., et al. (1989) J. Cell Biol. 109:1321.
9. Ugarova, T.P. et al. (1996) Biochemistry 35:10913.
10. Pytela, R. et al. (1985) Cell 40:191.
11. Abe, Y. et al. (2005) Biochem. Biophys. Res. Commun. 338:1640.

Publications for Fibronectin (3624-FN)(1)

Publication using 3624-FN

• Kato A, Okamoto O, Ishikawa K, Sumiyoshi H, Matsuo N, Yoshioka H, Nomizu M, Shimada T, Fujiwara S Dermatopontin interacts with fibronectin, promotes fibronectin fibril formation, and enhances cell adhesion. J. Biol. Chem., 2011-03-11;286(17):14861-9. 2011-03-11 [PMID: 21398523] (Bioassay, Human)

Bioinformatics

• Gene Symbol: FN1
• Uniprot:
  • NP_997647()