Vimentin plays a significant role in holding cellular structures of the organelles in the cytosol, and this protein has a flexible nature, allowing it to respond to mechanical stress. It interacts with other structural proteins, like microtubules, to make the cell rigid and sturdy. Studies performed on cells without vimentin found that they were functional, but very easily damaged when exposed to pressure. It was found that cells without vimentin are extremely delicate when disturbed with a micropuncture. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. As an organizer of a number of critical proteins, vimentin function involved in attachment, migration, and cell signaling.

Except for it maintains cellular integrity, stabilizes cytoskeleton interactions and provides resistance to avoid cells damage, vimentin also has an important clinical significance as a tumor marker. All intermediate filament proteins are expressed in a highly developmentally-regulated fashion; vimentin is the major cytoskeletal component of mesenchymal cells. vimentin is a widely expressed and highly conserved that is constitutively expressed in mesenchymal cells. Because of this, vimentin is often used as a marker of mesenchymally-derived cells or cells undergoing an epithelial-to-mesenchymal transition (EMT) during both normal development and metastatic progression. Vimentin IF proteins have been implicated in many aspects of cancer initiation and progression, including tumorigenesis, epithelial-to-mesenchymal transition, and the metastatic spread of cancer.

VIM antibody usually as a marker used for mesenchymal in histopathological diagnosis, and often with keratin to distinguish epithelial and mesenchymal tumors, such as identification of malignant melanoma, lymphoma and thymoma; VIM antibody and leukocyte common antigen to distinguish lymphoma and other mesenchymal tumors; VIM antibody and myogenic cell markers often identifiy myogenic and fibrous tumors, etc.