Vimentin Human

Vimentin is a class III intermediate filament protein predominantly found in cells of mesenchymal origin, such as vascular endothelium and blood cells . It plays a crucial role in maintaining cell integrity, providing resistance against stress, and supporting cellular structure . The human Vimentin protein is encoded by the VIM gene and consists of 466 amino acids . Recombinant human Vimentin is produced using advanced biotechnological methods to ensure high purity and functionality .

Recombinant human Vimentin is typically produced in Escherichia coli (E. coli) expression systems . The gene encoding human Vimentin is cloned into an expression vector, which is then introduced into E. coli cells. These cells are cultured under optimal conditions to express the Vimentin protein. After expression, the protein is purified using affinity chromatography techniques, often involving a His-tag for easy purification . The purified protein is then lyophilized and stored under specific conditions to maintain its stability and activity .

Vimentin is known to interact with various cellular components and participate in multiple biochemical processes. One notable interaction is with G-quadruplex (G4) structures, which are tetra-helical arrangements formed within guanine-rich tracts of DNA . Vimentin binds to these G4 structures with high affinity, potentially influencing gene expression and chromatin organization . Additionally, Vimentin plays a role in the epithelial-to-mesenchymal transition (EMT), a process critical for cancer metastasis and drug resistance . It interacts with various signaling molecules and structural proteins, contributing to cellular migration, division, and structural integrity .