Anti-Vinculin antibody, Mouse monoclonal clone VIN-11-5, purified from hybridoma cell culture

Anti-Vinculin antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the VIN-11-5 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a mouse immunized with smooth muscle vinculin from chicken gizzard. Vinculin, also known as metavinculin is highly conserved scaffolding protein localized to focal adhesions and adherens junctions. Vinculin is a 116 kDa protein with 1066 aminoacids. Vinculin comprises eight anti-parallel α-helical bundles organized into five distinct domains. Domains 1-3 are arranged into a tri-lobar head with a molecular mass of 95 kDa and diameter of 80Å . The vinculin head binds many proteins including talin, IpaA, β-catenin, α-catenin and α-actinin. A 61 amino acid, proline-rich linker region (residues 837-878) connects the head and tail. The linker binds vasodilator-stimulated phosphoprotein (VASP), vinexin, ponsin and Arp2/3. The vinculin tail (amino acids 879-1066) is a 30 kDa helical bundle containing five helices connected by short loops (3-8 residues). The tail contains binding sites for vinculin head domain, paxillin, acidic phospholipids and actin. Within the cell vinculin exists either as open, active form or as a closed, auto-inhibited state. The vinculin gene is mapped to human chromosome 10q22.2. Metavinculin (150 kDa), a splice variant of vinculin, is co-expressed with vinculin in muscle tissues. These proteins are localized to the cell membrane, the I-band in the sarcomere and to the intercalated discs.