Product nameAnti-Vinculin (phospho Y822) antibody
See all Vinculin primary antibodies
DescriptionRabbit polyclonal to Vinculin (phospho Y822)
Tested applicationsSuitable for: WBmore details
Species reactivityReacts with: Chicken
Predicted to work with: Mouse, Rat, Human
Synthetic peptide corresponding to Human Vinculin (phospho Y822). chemically synthesized phosphopeptide derived from a region of human vinculin that contains tyrosine 822.
Database link: P18206
- Chick Embryo Fibroblasts (CEFs) transfected with activated Src.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferpH: 7.3
Preservative: 0.05% Sodium azide
Constituents: 50% Glycerol, 0.1% BSA, 49% PBS
Concentration information loading...
PurityImmunogen affinity purified
Purification notesab200825 has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated vinculin. The final product is generated by affinity chromatography using a vinculin-derived peptide that is phosphorylated at tyrosine 822.
Our Abpromise guarantee covers the use of ab200825 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/1000. Predicted molecular weight: 124 kDa.|
FunctionActin 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.
Tissue specificityMetavinculin is muscle-specific.
Involvement in diseaseDefects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W) [MIM:611407]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Defects in VCL are the cause of cardiomyopathy familial hypertrophic type 15 (CMH15) [MIM:613255]. It is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.
Sequence similaritiesBelongs to the vinculin/alpha-catenin family.
DomainExists 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 takes on an 'active' conformation after cooperative and simultaneous binding of two different ligands. This activation involves displacement of the head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds a number of proteins that have both signaling and structural roles that are essential for cell adhesion.
The N-terminal globular head (Vh) comprises of subdomains D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links actin filaments into bundles. An intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt. The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt. Vt inhibits actin filament barbed end elongation without affecting the critical concentration of actin assembly.
modificationsPhosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1133 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques.
Aceylated; mainly by myristic acid but also small amount of palmitic acid.
Cellular localizationCytoplasm > cytoskeleton. Cell junction > adherens junction. Cell membrane. Cytoplasmic face of adhesion plaques. Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions.
- Information by UniProt
- CMD1W antibody
- CMH15 antibody
- Epididymis luminal protein 114 antibody
All lanes : Anti-Vinculin (phospho Y822) antibody (ab200825) at 1/1000 dilution
Lane 1 : Untransfected CEF lysates
Lane 2 : Src transfected CEF lysates
Lane 3 : Src transfected CEF lysates with non-phosphopeptide corresponding to immunogen
Lane 4 : Src transfected CEF lysates with generic phosphotyrosine containing peptide
Lane 5 : Src transfected CEF lysates with phosphopeptide immunogen
Lanes 1-2 : goat F(ab’)2 anti-rabbit IgG HRP conjugate
Developed using the ECL technique.
Predicted band size: 124 kDa
10% polyacrylamide gel transferred to PVDF blocked with a 5% BSA-TBST
ab200825 has not yet been referenced specifically in any publications.