Anti-Villin, clone VIL1/1314

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide. Recognizes a protein of ~93kDa which is identified as Villin (VIL1). It is a major constituent in the microvilli, which compose the brush border of epithelial cells forming absorptive surfaces of the intestinal and renal proximal tubular epithelia. Anti-Villin labels the brush border area in the gastrointestinal mucosal epithelium and urogenital tract. Among neoplasms, Villin is predominantly expressed in tumors of colorectal origin. Antibody to Villin is useful in identifying malignant cells from primary and metastatic colorectal carcinomas. This antibody also labels Merkel cells of the skin. 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]