Description
Vimentin is a cytoskeleton intermediate filament protein. It is composed of monomers that each contain a central α-helix rod domain, which facilitates formation of a coiled-coil dimer required for vimentin filament assembly, as well as N-terminal head and C-terminal tail domains. It is expressed in mesenchymal stem cells and cells of mesenchymal origin, including leukocytes, endothelial cells, and smooth muscle cells. 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. Vimentin controls transport of LDL-derived cholesterol from lysosomes to esterification sites. It is an aggresome component, forming a cage-like structure around aggregated, undegraded proteins at the microtubule organizing center. 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). ACPAs against citrullinated proteins, such as vimentin, are considered to be highly specific markers for rheumatoid arthritis and other autoimmune diseases. Cayman''s Vimentin Monoclonal Antibody (Clone 12E4) can be used for ELISA, immunoprecipitation (IP), and Western blot (WB) applications. The antibody recognizes vimentin at approximately 54 kDa from human samples.
References
[1] JOHN E ERIKSSON. Introducing intermediate filaments: from discovery to disease.[J]. The Journal of clinical investigation, 2009: 1763-1771. DOI:
10.1172/jci38339[2] LYNNE CHANG. Assembling an intermediate filament network by dynamic cotranslation.[J]. Journal of Cell Biology, 2006, 172 5: 747-758. DOI:
10.1083/jcb.200511033[3] De Souza, F.I., Zumiotti, A.V., and Da Silva, C.F. Neuregulins 1-α and 1-β on the regeneration the peripheral nerves[J]. Acta Ortop Bras.
[4] A J SARRIA R M E S R Panini. A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells.[J]. The Journal of Biological Chemistry, 1992, 267 27: 19455-19463.
[5] J A JOHNSTON R R K C L Ward. Aggresomes: a cellular response to misfolded proteins.[J]. Journal of Cell Biology, 1998, 143 7: 1883-1898. DOI:
10.1083/jcb.143.7.1883[6] LILLA SOóS. Clinical evaluation of anti-mutated citrullinated vimentin by ELISA in rheumatoid arthritis.[J]. Journal of Rheumatology, 2007, 34 8: 1658-1663.
[7] HIROAKI ASAGA Tatsuo S Michiyuki Yamada. Selective Deimination of Vimentin in Calcium Ionophore-Induced Apoptosis of Mouse Peritoneal Macrophages[J]. Biochemical and biophysical research communications, 1998, 243 3: Pages 641-646. DOI:
10.1006/bbrc.1998.8148
