Vimentin is a class III intermediate filament protein predominantly found in cells of mesenchymal origins, such as vascular endothelium and blood cells, where it functions as a major cytoskeletal component. Due to its importance and abundance in the cytoskeletal structure of mesenchymally-derived cells, Vimentin is frequently used as a developmental marker within cells of mesenchymal origin or cells undergoing epithelial-mesenchymal transition, which can occur during both normal and metastatic growth. An active participant within several critical processes of cellular organization and protein regulation, Vimentin is involved in the anchorage of organelles within the cytoplasmic matrix, development of astrocytes, and the disassembly of cellular components during the execution phase of apoptosis. Abnormalities in the normal physiological pathways of Vimentin have been implicated in deficient motility and directional migration involved in wound healing and cellular growth and development, as well as the adhesion-site accumulation of Vimentin on lens epithelial cells in cases of dominant cataracts. Recombinant Human Vimentin is a 54.5 kDa protein consisting of 472 amino acid residues, including a 6 residue C-terminal His-Tag.