Monoclonal Anti-Vinculin (mouse IgG1 isotype) is derived from the hVIN-1 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from immunized BALB/c mice. Vinculin is localized in the fascia adherens of the intercalated disk (cardiac muscle), myotendinous junctions (skeletal muscle), neuromuscular junctions and the membrane-associated dense bodies of smooth muscle. In many cell types undergoing viral transformation, vinculin becomes redistributed to rosettes or podosomes.
Monoclonal Anti-Vinculin specifically stains vinculin at cell-cell and cell-substrate contacts in tissue and cultured cells using indirect immunofluorescent labeling. The antibody reacts with the 116 kDa vinculin band in immunoblotting. The product reacts with vinculin of many species. Good reactivity is obtained with human, bovine, chicken, dog, rat, mouse, turkey, and Xenopus. The antibody shows cross reactivity with smooth muscle metavinculin.
Specifically labels vinculin at cell-cell and cell-substrate contacts. Reacts strongly with human vinculin. Shows cross-reactivity with smooth muscle metavinculin.
purified human vinculin from uterus.
Monoclonal Anti-Vinculin antibody produced in mouse has been used in:
- western blotting
- immunofluorescence staining
Vinculin is a cytoskeletal protein associated with the cytoplasmic faces of both cell-cell and cell-extracellular matrix adherens-type junctions. It functions as one of several interacting proteins involved in anchoring F-actin to the membrane. A sequence of molecular interactions might be involved in the transmembrane assembly of adhesion plaques. In the assembly of adhesion plaques, the β-subunit of integrin binds to talin. Talin binds to vinculin that interacts with α-actinin and possibly with itself. Since α-actinin binds to and cross-links actin filaments, vinculin represents a key element in the transmembrane linkage of the extracellular matrix to the cytoplasmic microfilament system.
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