Anti Vinculin Antibody

Vinculin (VCL) is a cytoskeleton protein that is closely related to cell-matrix interactions and cell-cell junctions. VCL is a membrane-cytoskeleton protein in focal adhesion plates that are involved in the binding of integrin adhesion molecules to the actin cytoskeleton. The protein contains an N-terminal acid domain and a C-terminal basic domain separated by a proline-rich middle segment.

Extensive species reactivity highly cited and reviewed Vinculin Antibody. Guaranteed specificity. See datasheets. Technical support. Knockout validated. Available trial sizes. Kits and Tests. Highlights: Online registration options available, Online purchase options available at Bosterbio.com.

This protein has multi-ligand properties and has been found to interact with various microfilament-associated proteins, such as talin, a-actinin, and paxillin, which are reported to bind to the head or tail domains of vinculin.

Vinculin is a cytoskeleton protein associated with cell-cell and matrix-cell junctions, where it is believed to function as one of several interacting proteins involved in anchoring F-actin to the membrane. VCL defects are the cause of type 1W dilated cardiomyopathy.

Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, leading to congestive heart failure and arrhythmia. Multiple alternatively spliced ​​transcript variants have been found for this gene, but the biological validity of some variants has not been determined.

Actin filament-binding protein (F-actin) involved in cell-matrix adhesion and cell-to-cell adhesion. Regulates the expression of E-cadherin on the cell surface and enhances mechanosensitivity through the E-cadherin complex. It can also play important roles in cell morphology and locomotion.

VCL defects are the cause of type 1W dilated cardiomyopathy (CMD1W) [MIM: 611407]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, leading to congestive heart failure and arrhythmia. Patients are at risk of premature death.

VCL defects are the cause of familial hypertrophic cardiomyopathy type 15 (CMH15) [MIM: 613255]. It is an inherited heart disorder characterized by ventricular hypertrophy, which is generally asymmetric and often involves the ventricular septum.

Symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be easily triggered by exercise. The disorder has inter- and intra-family variability that varies from benign to malignant forms with a high risk of heart failure and sudden cardiac death.

It exists in at least two conformations. When in the closed, 'inactive' conformation, extensive interactions between the head and tail domains prevent detectable binding to most of its ligands. It assumes an "active" conformation after the simultaneous and cooperative binding of two different ligands.

This activation involves the displacement of head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds various proteins that have signaling and structural functions that are essential for cell adhesion.

The N-terminal globular head (Vh) is made up of D1-D4 subdomains. The C-terminal tail (Vt) binds actin F and crosslinks the actin filaments into bundles. An intramolecular interaction between Vh and Vt masks the actin-binding domain F located in Vt.

The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical conversion of this subdomain, leading to disruption of intramolecular interaction and exposure of the cryptic domain of F-actin binding of Vt. Vt inhibits the actin filament by lengthening the barbed end without affecting the critical concentration of the actin assembly.

Phosphorylated; in serines, threonines, and tyrosines. Tyr-1133 phosphorylation in activated platelets affects head-tail interactions and cell propagation but has no effect on actin-binding or localization on focal adhesion plates.

Acetylated; mainly myristic acid, but also a small amount of palmitic acid.

Cytoplasm> cytoskeleton. Cellular junction> adherent junction. Cellular membrane. The cytoplasmic face of the adhesion plates. Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization at cell-cell junctions.