Anti-Villin (Clone: ABM4E64)

Villin is a protein that belongs to the gelsolin family of calcium-regulated actin-binding proteins. It is expressed in differentiated epithelial cells with a brush border such as intestinal villi, proximal renal tubules, oviduct, and seminiferous ducts. Villin shares structural and functional homology with two conserved families of proteins. One family of proteins, which includes gelsolin and adseverin, shares the conserved domain(s) found in the villin core. Villin regulates cell migration, cell death, and epithelial-to-mesenchymal transition underscoring the significance of this protein to epithelial cell function. Protein function: Epithelial cell-specific Ca(2+)-regulated actin- modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA), binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination. [The UniProt Consortium]