Application

Anti-Vinculin antibody, Mouse monoclonal has been used in immunoblotting immunofluorescence staining immunocytochemistryimmunohistochemistry and enzyme linked immunosorbent assay (ELISA).

Biochem/physiol Actions

Vinculin functions as one of several interacting proteins involved in anchoring F-actin to the membrane. It has been shown that a sequence of molecular interactions might be involved in the transmembrane assembly of adhesion plaques. vinculin represents a key element in the transmembrane linkage of the extracellular matrix to the cytoplasmic microfilament system. In many cell types undergoing viral transformation, vinculin becomes redistributed to rosettes or podosomes.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

Anti-Vinculin antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hVIN-1 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with vinculin purified from human uterus. Vinculin is a cytoskeletal protein associated with the cytoplasmic faces of both cell-cell and cell-extracellular matrix adherens-type junctions. In muscle, 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.

Immunogen

purified human vinculin from uterus.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Specificity

Specifically labels vinculin at cell-cell and cell-substrate contacts. Reacts strongly with human vinculin. Shows cross-reactivity with smooth muscle metavinculin.