Pricing updated 2019-03-21. Prices are subject to change without notice.
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.
View the Cayman Structure Database for chemical structure definitions for many Cayman products
Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data pack, and GC-MS data.
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).
Chang, L., Shav-
Sarria, A.J., Panini, S.R., and Evans, R.M. A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-
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).
Soós, L., Szekanecz, Z., Szabó, Z., et al. Clinical evaluation of anti-
Asaga, H., Yamada, M., and Senshu, T. Selective deimination of vimentin in calcium ionophore-