The Vimentin protein is a 57 kDa class III intermediate filament (IF) protein that belongs to the intermediate filament family. Vimentin is the predominant intermediate filament in cells of mesenchymal origin such as vascular endothelium and blood cells (1-3). The human Vimentin cDNA encodes a 466 amino acid (aa) Vimentin protein that contains head and tail regions with multiple regulatory Ser/Thr phosphorylation sites, and a central rod domain with three coiled-coil regions separated by linkers (1, 2). The human Vimentin protein shares 97-98% aa identity with the mouse, rat, bovine and canine Vimentin proteins. Sixteen Vimentin coiled-coil dimers self-assemble to form intermediate (10-12 nm wide) filaments (4). These filaments then anneal longitudinally to form non-polarized fibers that support cell structure and withstand stress (4). Intermediate filament fibers are highly dynamic, and their half-life depends on the balance between kinase and phosphatase activity. For example, phosphorylation followed by dephosphorylation drives intermediate filament disintegration, followed by reorganization during mitosis (1, 5, 6). Interactions of head and tail domains link intermediate filaments with other structures such as actin and microtubule cytoskeletons (7). The Vimentin protein is involved in positioning autophagosomes, lysosomes and the Golgi complex within the cell (8). It facilitates cell migration and motility by recycling internalized trailing edge integrins back to the cell surface at the leading edge (9-11). Vimentin also helps maintain the lipid composition of cellular membranes, and caspase cleavage of the Vimentin protein is a key event in apoptosis (8, 12). Phosphorylation of the Vimentin protein promotes its secretion by TNF-alpha -stimulated macrophages (13). Extracellular Vimentin has been shown to associate with several microbes, and appears to promote an antimicrobial oxidative burst (13, 14). Cell-associated Vimentin can also interact with NKp46 to recruit NK cells to tuberculosis-infected monocytes (15).
Recombinant Human Vimentin Protein, CF
R&D Systems | Catalog # 2105-VI
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Key Product Details
- R&D Systems E. coli-derived Recombinant Human Vimentin Protein (2105-VI)
- Quality control testing to verify active proteins with lot specific assays by in-house scientists
- All R&D Systems proteins are covered with a 100% guarantee
Source
E. coli
Accession Number
Applications
Binding Activity
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Product Specifications
Source
E. coli-derived human Vimentin protein
Ser2-Glu466, with a C-terminal 6-His tag
Ser2-Glu466, with a C-terminal 6-His tag
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal Sequence Analysis
Ser2
Predicted Molecular Mass
54.4 kDa
Activity
Measured by its ability to bind Recombinant Human NKp46/NCR1 Fc Chimera (Catalog # 1850-NK) in a functional ELISA with an estimated KD < 2 nM. Garg, A. et al. (2006) J. Immunol. 177:6192.
Formulation, Preparation, and Storage
2105-VI
| Formulation | Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with Trehalose. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile 4 mM HCl.
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| 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.
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Calculators
Background: Vimentin
References
- Omary, M.B. et al. (2006) Trends Biochem. Sci. 31:383.
- Ivaska, J. et al. (2007) Exp. Cell Res. 313:2050.
- Ferrari, S. et al. (1986) Mol. Cell. Biol. 6:3614.
- Sokolova, A.V. et al. (2006) Proc. Natl. Acad. Sci. USA 103:16206.
- Eriksson, J.E. et al. (2004) J. Cell Sci. 117:919.
- Li, Q.-F. et al. (2006) J. Biol. Chem. 281:34716.
- Esue, O. et al. (2006) J. Biol. Chem. 281:30393.
- Styers, M.L. et al. (2005) Traffic 6:359.
- McInroy, L. and A. Maata (2007) Biochem. Biophys. Res. Commun. 360:109.
- Nieminen, M. et al. (2006) Nat. Cell Biol. 8:156.
- Ivaska, J. et al. (2005) EMBO J. 24:3834.
- Byun, Y. et al. (2001) Cell Death Differ. 8:443.
- Mor-Vaknin, N. et al. (2003) Nat. Cell Biol. 5:59.
- Zou, Y. et al. (2006) Biochem. Biophys. Res. Commun. 351:625.
- Garg, A. et al. (2006) J. Immunol. 177:6192.
Alternate Names
VIM
Gene Symbol
VIM
UniProt
Additional Vimentin Products
Product Documents for Recombinant Human Vimentin Protein, CF
Certificate of Analysis
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Note: Certificate of Analysis not available for kit components.
Product Specific Notices for Recombinant Human Vimentin Protein, CF
For research use only
Citations for Recombinant Human Vimentin Protein, CF
Customer Reviews for Recombinant Human Vimentin Protein, CF (1)
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Sample Tested: Purified proteinVerified Customer | Posted 10/26/2015We are testing this protein as a positive control and it works flawlessly. <br />Specificity: Specific<br />Sensitivity: Sensitive<br />Buffer: Loading buffer<br />Dilution: 1 ng
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