Anti-Vinculin

0.5mg/ml if reconstituted with 0.2ml sterile DI water. In mammalian cells, Vinculin is a membrane-cytoskeletal protein in focal adhesion plaques that is involved in linkage of integrin adhesion molecules to the actin cytoskeleton. By linkage studies in a 3-generation family, Mulligan et al.(1992) mapped the VCL gene to chromosome 10q22.1-q23, distal to D10S22. It is a cytoskeletal protein associated with cell-cell and cell-matrix junctions, where it is though to function as one of several interacting proteins involved in anchoring F-actin to the membrane. Multiple alternatively-spliced transcript variants have been found for this gene, but the biological validity of some variants has not been determined. The human protein exhibits a greater-than-95% sequence identity to the chicken protein. Vinculin is a 117-kDa cytoskeletal protein with 1066 amino acids. The protein contains an acidic N-terminal domain and a basic C-terminal domain separated by a proline-rich middle segment. It has a globular head domain that contains binding sites for talin and alpha-actinin as well as a tyrosine phosphorylation site, while the tail region contains binding sites for F-actin, paxillin, and lipids. Protein function: Actin filament (F-actin)-binding protein involved in cell- matrix adhesion and cell-cell adhesion. Regulates cell-surface E- cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. [The UniProt Consortium]