Vimentin Polyclonal Antibody

Vimentin is a cytoskeleton intermediate filament protein.¹ 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.^1,2 It is expressed in mesenchymal stem cells and cells of mesenchymal origin, including leukocytes, endothelial cells, and smooth muscle cells.³ 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.⁴ It is an aggresome component, forming a cage-like structure around aggregated, undegraded proteins at the microtubule organizing center.⁵ 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).^6,7 ACPAs against citrullinated proteins, such as vimentin, are considered to be highly specific markers for rheumatoid arthritis and other autoimmune diseases.⁶ Cayman's Vimentin Monoclonal Antibody (Clone 12E4) can be used for ELISA and Western blot (WB) applications. The antibody recognizes vimentin at approximately 54 kDa from human samples.

WARNING This product is not for human or veterinary use.

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. Franke, W.W., Grund, C., Kuhn, C., et al. Formation of cytoskeletal elements during mouse embryogenesis. III. Primary mesenchymal cells and the first appearance of vimentin filaments. Differentiation 23(1), 43-59 (1982).

4. 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).

5. 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).

6. 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).

7. 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).