Host: E. coli • AA: 1-466 (full length) • MW: 53.75 kDa
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Citrullinated Vimentin (G147R mutant; human, recombinant)

Item No. 46119

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Purity
≥70% estimated by SDS-PAGE
Source
Recombinant human vimentinG147R expressed in E. coli and citrullinated by PAD2
Amino Acids
1-466 (full length)
MW
53.75 kDa
Formulation (Request formulation change)
10 mM Tris, pH 7.5
UniProt Accession №
P08670
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

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    100 µg

    $499

    Add
    Cayman Chemical
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    Product Description

    Vimentin is a cytoskeletal intermediate filament protein present in cells of mesenchymal origin, including leukocytes, endothelial cells, and smooth muscle cells.1 It is subject to citrullination by peptidyl arginine deiminase 2 (PAD2; Item No. 10785) under high calcium concentrations, which can occur during macrophage apoptosis.2 Citrullinated vimentin has been shown to have a role in the production of anti-citrullinated protein antibodies (ACPAs).3,2 Serum levels of immune complexes targeting citrullinated vimentin are increased in patients with rheumatoid arthritis and positive for ACPAs.4 Serum and plasma levels of citrullinated vimentin are also increased in patients with lung cancer or idiopathic pulmonary fibrosis, respectively.5,6 Citrullinated vimentin containing a glycine-to-arginine substitution (vimentinG147R) has been found in isolated human synovial fluid.7 VimentinG147R has increased antigenicity compared with wild-type vimentin in serum from patients with rheumatoid arthritis. Cayman's Citrullinated Vimentin (G147R; human, recombinant) protein is derived from purified Vimentin (G147R mutant; human, recombinant) (Item No. 45102) that has been modified by PAD2 (Item No. 10785), which was removed by affinity chromatography after the reaction.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Ivaska, J., Pallari, H.-M., Nevo, J., et al. Novel functions of vimentin in cell adhesion, migration, and signaling. Exp. Cell Res. 313(10), 2050-2062 (2007).

    2. 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).

    3. 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).

    4. Van Steendam, K., Tilleman, K., De Ceuleneer, M., et al. Citrullinated vimentin as an important antigen in immune complexes from synovial fluid of rheumatoid arthritis patients with antibodies against citrullinated proteins. Arthritis Res. Ther. 12(4), R132 (2010).

    5. Willumsen, N., Bager, C.L., Leeming, D.J., et al. Serum biomarkers reflecting specific tumor tissue remodeling processes are valuable diagnostic tools for lung cancer. Can. Med. 3(5), 1136-1145 (2014).

    6. Li, F.J., Surolia, R., Li, H., et al. Autoimmunity to vimentin is associated with outcomes of patients with idiopathic pulmonary fibrosis. J. Immunol. 199(5), 1596-1605 (2017).

    7. Bang, H., Egerer, K., Gauliard, A., et al. Mutation and citrullination modifies vimentin to a novel autoantigen for rheumatoid arthritis. Arthritis Rheum. 56(8), 2503-2511 (2007).