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Recombinant Human Vimentin Protein, CF Best Seller

Bio-Techne includes R&D Systems | Catalog # 2105-VI

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2105-VI-100

Key Product Details

Source

E. coli

Accession #

Conjugate

Unconjugated

Applications

Binding Activity

Product Specifications

Source

E. coli-derived human Vimentin protein
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 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.
  • 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.

Background: Vimentin

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).

References

  1. Omary, M.B. et al. (2006) Trends Biochem. Sci. 31:383.
  2. Ivaska, J. et al. (2007) Exp. Cell Res. 313:2050.
  3. Ferrari, S. et al. (1986) Mol. Cell. Biol. 6:3614.
  4. Sokolova, A.V. et al. (2006) Proc. Natl. Acad. Sci. USA 103:16206.
  5. Eriksson, J.E. et al. (2004) J. Cell Sci. 117:919.
  6. Li, Q.-F. et al. (2006) J. Biol. Chem. 281:34716.
  7. Esue, O. et al. (2006) J. Biol. Chem. 281:30393.
  8. Styers, M.L. et al. (2005) Traffic 6:359.
  9. McInroy, L. and A. Maata (2007) Biochem. Biophys. Res. Commun. 360:109.
  10. Nieminen, M. et al. (2006) Nat. Cell Biol. 8:156.
  11. Ivaska, J. et al. (2005) EMBO J. 24:3834.
  12. Byun, Y. et al. (2001) Cell Death Differ. 8:443.
  13. Mor-Vaknin, N. et al. (2003) Nat. Cell Biol. 5:59.
  14. Zou, Y. et al. (2006) Biochem. Biophys. Res. Commun. 351:625.
  15. Garg, A. et al. (2006) J. Immunol. 177:6192.

Alternate Names

VIM

Entrez Gene IDs

7431 (Human); 22352 (Mouse); 81818 (Rat)

Gene Symbol

VIM

UniProt

Additional Vimentin Products

Product Documents for Recombinant Human Vimentin Protein, CF

Certificate of Analysis

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Product Specific Notices for Recombinant Human Vimentin Protein, CF

For research use only

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  • Recombinant Human Vimentin Protein, CF
    Name: Anonymous
    Sample Tested: Purified protein
    Verified Customer | Posted 10/26/2015
    We are testing this protein as a positive control and it works flawlessly.
    Specificity: Specific
    Sensitivity: Sensitive
    Buffer: Loading buffer
    Dilution: 1 ng
    Recombinant Human Vimentin Protein, CF 2105-VI

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