Purified, recombinant protein
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Vimentin (human, recombinant)

Item No. 11234

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Purity
≥90% estimated by SDS-PAGE
Source
Recombinant N-terminal histidine-tagged vimentin purified from E. coli
Amino Acids
2-466
MW
55.2 kDa
Formulation (Request formulation change)
10 mM Tris, pH 8.0
UniProt Accession №
P08670
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $528

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    Product Description

    Vimentin is a cytoskeleton intermediate filament protein present in cells of mesenchymal origin, including leukocytes, endothelial cells, and smooth muscle cells.1 Each vimentin monomer contains a central α-helix that facilitates formation of the coil-coil dimer required for vimentin filament assembly.2 Vimentin is attached to nuclei, endoplasmic reticulum, and mitochondria, and has a role in positioning organelles in the cytosol. It regulates glial morphology, facilitates motility and directional migration of fibroblasts, and is critical to mechanotransduction of shear stress and maintenance of vascular endothelial integrity.1 Vimentin controls transport of LDL-derived cholesterol from lysosomes to esterification sites.3 It is an aggresome component, forming a cage-like structure around aggregated, undegraded proteins at the microtubule organizing center.4 Vimentin is subject to citrullination under high calcium concentrations, which can occur during macrophage apoptosis, and citrullinated vimentin has been shown to have a role in the production of anti-citrullinated protein antibodies (ACPAs).5,6 ACPAs against citrullinated proteins, such as vimentin, are considered to be highly specific markers for rheumatoid arthritis and other autoimmune diseases.5

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Eriksson, J.E., Dechat, T., Grin, B., et al. Introducing intermediate filaments: From discovery to disease. J. Clin. Invest. 119(7), 1763-1771 (2009).

    2. Chang, L., Shav-Tal, Y., Trcek, T., et al. Assembling an intermediate filament network by dynamic cotranslation. J. Cell. Biol. 172(5), 747-758 (2006).

    3. Sarria, A.J., Panini, S.R., and Evans, R.M. A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells. The Journal of Biological Chemisty 267(27), 19455-19463 (1992).

    4. Johnston, J.A., Ward, C.L., and Kopito, R.R. Aggresomes: A cellular response to misfolded proteins. J. Cell Biol. 143(7), 1883-1898 (1998).

    5. Soós, L., Szekanecz, Z., Szabó, Z., et al. Clinical evaluation of anti-mutated citrullinated vimentin by ELISA in rheumatoid arthritis. J. Rheumatol. 34(8), 1658-1663 (2007).

    6. Asaga, H., Yamada, M., and Senshu, T. Selective deimination of vimentin in calcium ionophore-induced apoptosis of mouse peritoneal macrophages. Biochem. Biophys. Res. Commun. 243(3), 641-646 (1998).

    Product Citations

    Moon, J.-S., Younis, S., Ramadoss, N.S., et al. Cytotoxic CD8+ T cells target citrullinated antigens in rheumatoid arthritis. Nat. Commun. 14(1), 319 (2023).