Phospho-Vimentin (Ser39) Rabbit Polyclonal Antibody

Phospho-Vimentin (Ser39) refers to the phosphorylation modification of the intermediate filament protein vimentin at serine residue 39, serving as a core molecular switch regulating dynamic cytoskeletal remodeling. Vimentin is the major type III intermediate filament protein in mesenchymal cells, and its Ser39 site is located within the head domain that is critical for filament assembly. Phosphorylation at this site induces conformational changes that weaken filament-filament interactions, thereby promoting intermediate filament disassembly or reorganization—a dynamic process that is particularly crucial during mitosis, cell migration, and in response to mechanical stress. At the level of signal regulation, phosphorylation at this site is precisely controlled by multiple kinases. For example, the AKT1 pathway can mediate its phosphorylation, thereby affecting cell motility, and this phosphorylation modification can also protect vimentin from proteolysis, enhancing its function in regulating cell migration. Dysregulation of this modification has significant pathological implications: in Treponema pallidum infection, the pathogen can disrupt the fibronectin matrix barrier by inducing phosphorylation at Ser39 in vascular endothelial cells, promoting its own dissemination; in cancer research, elevated phosphorylation at this site is closely associated with epithelial-mesenchymal transition (EMT), cancer cell invasion, and poor prognosis, while also playing important roles in physiological processes such as copper-promoted migration of adipose-derived stem cells.