Recombinant Human Vimentin Protein, CF

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2105-VI-100
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Citations (7)
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Recombinant Human Vimentin Protein, CF Summary

Product Specifications

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.
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.
Source
E. coli-derived human Vimentin protein
Ser2-Glu466, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Ser2
Predicted Molecular Mass
54.4 kDa

Product Datasheets

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2105-VI

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. 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 could interfere.

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.
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.
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Reconstitution Calculator

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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.
Entrez Gene IDs
7431 (Human); 22352 (Mouse); 81818 (Rat)
Alternate Names
epididymis secretory sperm binding protein; FLJ36605; VIM; Vimentin

Citations for Recombinant Human Vimentin Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

7 Citations: Showing 1 - 7
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  1. Identification of anti-citrullinated osteopontin antibodies and increased inflammatory response by enhancement of osteopontin binding to fibroblast-like synoviocytes in rheumatoid arthritis
    Authors: A Umemoto, T Kuwada, K Murata, M Shiokawa, S Ota, Y Murotani, A Itamoto, K Nishitani, H Yoshitomi, T Fujii, A Onishi, H Onizawa, K Murakami, M Tanaka, H Ito, H Seno, A Morinobu, S Matsuda
    Arthritis Research & Therapy, 2023-02-17;25(1):25.
    Species: Human, N/A
    Sample Types: Antibody, Protein, Whole Cells
    Applications: Bioassay, ELISA Capture
  2. Autophagy promotes citrullination of VIM (vimentin) and its interaction with major histocompatibility complex class II in synovial fibroblasts
    Authors: E Sugawara, M Kato, Y Kudo, W Lee, R Hisada, Y Fujieda, K Oku, T Bohgaki, O Amengual, S Yasuda, T Onodera, S Hatakeyama, T Atsumi
    Autophagy, 2019-09-08;0(0):1-10.
    Species: Human
    Sample Types: Serum
    Applications: Western Blot
  3. Cigarette Smoke Induces Immune Responses to Vimentin in both, Arthritis-Susceptible and -Resistant Humanized Mice
    PLoS ONE, 2016-09-07;11(9):e0162341.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  4. Potential Function of Exogenous Vimentin on the Activation of Wnt Signaling Pathway in Cancer Cells
    J Cancer, 2016-08-12;7(13):1824-1832.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. The mosaic of "seronegative" antiphospholipid syndrome.
    Authors: Conti F, Capozzi A, Truglia S, Lococo E, Longo A, Misasi R, Alessandri C, Valesini G, Sorice M
    J Immunol Res, 2014-03-17;2014(0):389601.
    Species: Human
    Sample Types: Serum
    Applications: Bioassay
  6. Universal marker and detection tool for human sarcoma circulating tumor cells.
    Authors: Satelli A, Mitra A, Cutrera J, Devarie M, Xia X, Ingram D, Dibra D, Somaiah N, Torres K, Ravi V, Ludwig J, Kleinerman E, Li S
    Cancer Res, 2014-01-21;74(6):1645-50.
    Species: Human
    Sample Types: Serum
    Applications: Bioassay
  7. Vimentin/cardiolipin complex as a new antigenic target of the antiphospholipid syndrome.
    Authors: Ortona E, Capozzi A, Colasanti T, Conti F, Alessandri C, Longo A, Garofalo T, Margutti P, Misasi R, Khamashta MA, Hughes GR, Valesini G, Sorice M
    Blood, 2010-07-15;116(16):2960-7.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Binding Assay

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Recombinant Human Vimentin Protein, CF
By Anonymous on 10/26/2015
Sample Tested: Purified protein

We are testing this protein as a positive control and it works flawlessly.
Specificity: Specific
Sensitivity: Sensitive
Buffer: Loading buffer
Dilution: 1 ng