Recombinant Human Fibronectin/Anastellin Protein, CF Summary
Details of Functionality |
Measured by the ability of the immobilized protein to enhance Fibronectin-mediated adhesion of NIH‑3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 0.3-1.5 μg/mL. |
Source |
E. coli-derived human Fibronectin/Anastellin protein Asn631-Pro705, with an N-terminal Met and a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Met & Asn631 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
FN1 |
Purity |
>95%, by SDS-PAGE with silver staining |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
9 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 |
9 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 with silver staining |
Reconstitution Instructions |
Reconstitute at 250 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Fibronectin/Anastellin Protein, CF
Background
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). 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. 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 the sensitivity to proteases (6, 7). A fragment from the first type III repeat, known as Anastellin, binds to fibronectin and induces the formation of high molecular weight disulfide-linked superfibronectin (sFN) (8-10). sFN exhibits increased protease sensitivity and cellular adhesiveness compared to fibronectin (8, 10). Anastellin acts
in vivo to inhbit angiogenesis, tumor growth, and metastasis (9).
- Mao, Y. and Schwarzbauer, J.E. (2005) Matrix Biol. 24:389.
- Potts, J.R. and Campbell, I.D. (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.
- Morla, A. et al. (1994) Nature 367:193.
- Yi, M. and E. Rouslahti (2001) Proc. Natl. Acad. Sci. USA 98:620.
- Ohashi, T. and H.P. Erickson (2005) J. Biol. Chem. 280:39143.
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