Bovine vimentin, like other vimentin proteins, is composed of a central α-helical rod domain flanked by non-helical head and tail domains. This structure allows vimentin to form coiled-coil dimers, which further assemble into tetramers and ultimately into intermediate filaments. The molecular weight of bovine vimentin is approximately 57 kDa .
Vimentin is essential for several cellular functions:
Vimentin is developmentally regulated and is expressed during the early stages of cellular development. It is co-expressed with desmin in certain cell types. The expression of vimentin can be influenced by cellular density, drug delivery algorithms, and treatments such as chemotherapy and radiotherapy .
Vimentin has significant implications in medical research and diagnostics:
Bovine vimentin is widely used in research to study its role in cellular processes and disease mechanisms. Recombinant bovine vimentin protein is produced and utilized in various laboratory applications, including immunization and structural studies .
In conclusion, bovine vimentin is a vital intermediate filament protein with diverse roles in cellular structure, function, and disease. Its study continues to provide valuable insights into cell biology and potential therapeutic approaches for various diseases.