For immunochemical detection of citrullinated vimentin
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Citrullinated Vimentin Monoclonal Antibody (Clone 12G11)

Item No. 22054

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Immunogen
Synthetic peptide from human vimentin with citrullines at 145 and 147 (G147R mutation)
Clone Designation
12G11
Formulation (Request formulation change)
100 µg of protein G-purified antibody
Storage Buffer
PBS, pH 7.2, with 0.02% sodium azide (avoid freeze/thaw cycles)
Host
Mouse
Isotype
IgG1
Applications
ELISA, WB, and IP
Cross Reactivity
(+) Citrullinated vimentin(-) Unmodified protein
Species Reactivity
(+) Human; other species not tested
UniProt Accession №
P08670
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

Download most recent Certificate of Analysis for this product

    100 µg

    $440

    Add
    Cayman Chemical
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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. It is subject to citrullination by peptidyl arginine deiminase 2 (PAD2; Item No. 10785) under high calcium concentrations, which can occur during macrophage apoptosis.1 Citrullinated vimentin has been shown to have a role in the production of anti-citrullinated protein antibodies (ACPAs).2,1 Serum levels of immune complexes targeting citrullinated vimentin are increased in patients with rheumatoid arthritis and positive for ACPAs.3 Serum and plasma levels of citrullinated vimentin are also increased in patients with lung cancer or idiopathic pulmonary fibrosis, respectively.4,5 Cayman's Citrullinated Vimentin Monoclonal Antibody (Clone 12G11) can be used for ELISA, immunoprecipitation (IP), and Western blot (WB) applications. The antibody recognizes citrullinated vimentin at approximately 54 kDa from human samples.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. 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).

    2. 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).

    3. 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).

    4. 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).

    5. 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).

    Product Citations

    Song, Y.N., Zhang, F., He, Y., et al. Berberine inhibits protein citrullination of fibroblast-like synoviocytes by suppressing autophagy via STAT3/PAD4 pathway. Phytomedicine 150:157706, (2026).

    Gorzeń, O., Mikołajczyk-Martinez, A., Mamun, A.A., et al. Isoform-selective PAD2/PAD4 substrates with unnatural amino acids enable cellular peptidylarginine deiminase activity profiling and reveal vimentin citrullination effects in macrophages. Biochemistry 64(19), 4105-4120 (2025).

    Sugawara, E., Kato, M., Kudo, Y., et al. Autophagy promotes citrullination of VIM (vimentin) and its interaction with major histocompatibility complex class II in synovial fibroblasts. Autophagy 16(5), 946-955 (2020).

    Morin-Genest, J., and Girard, D. Citrullinated vimentin and alpha enolase are expressed at the cell surface of apoptotic human neutrophils. Hum. Immunol. 87(1), 111631 (2026).