Product Specifications for Recombinant Human Vimentin Protein, CF
E. coli-derived human Vimentin protein Ser2-Glu466, with a C-terminal 6-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis
Predicted Molecular Mass
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
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant
protein to be stored at a more dilute concentration.
The carrier free version does not contain BSA.
What formulation is right for me?
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or
as an ELISA standard.
In contrast, the carrier free protein is recommended for applications, in which the presence of BSA
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Reconstitute at 100 μg/mL in sterile 4 mM HCl.
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.
Vimentin is a 57 kDa class III intermediate filament (IF) protein that belongs to the intermediate filament family. It is the predominant IF in cells of mesenchymal origin such as vascular endothelium and blood cells (1-3). The human Vimentin cDNA encodes a 466 amino acid (aa) 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). Human Vimentin shares 97-98% aa identity with mouse, rat, ovine, bovine and canine Vimentin. 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). IF fibers are highly dynamic, and half-life depends on the balance between kinase and phosphatase activity. For example, phosphorylation followed by dephosphorylation drives IF disintegration, followed by reorganization during mitosis (1, 5, 6). Interactions of head and tail domains link IFs with other structures such as actin and microtubule cytoskeletons (7). Vimentin 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 helps maintain the lipid composition of cellular membranes, and caspase cleavage of Vimentin is a key event in apoptosis (8, 12). Phosphorylation promotes secretion of Vimentin 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).
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Ivaska, J. et al. (2007) Exp. Cell Res. 313:2050.
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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.
Entrez Gene IDs
7431 (Human); 22352 (Mouse); 81818 (Rat)
FLJ36605, VIM, Vimentin, epididymis secretory sperm binding protein
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