Product: Phospho-Vinculin (Tyr822) Antibody
Catalog: AF3206
Description: Rabbit polyclonal antibody to Phospho-Vinculin (Tyr822)
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 123kDa; 124kD(Calculated).
Uniprot: P18206
RRID: AB_2834638

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 100ul $280 In stock
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Product Info

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Pig(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%)
Phospho-Vinculin (Tyr822) Antibody detects endogenous levels of Vinculin only when phosphorylated at Tyrosine 822.
Cite Format: Affinity Biosciences Cat# AF3206, RRID:AB_2834638.
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


CMD1W; CMH15; Epididymis luminal protein 114; HEL114; Metavinculin; MV; MVCL; OTTHUMP00000019861; OTTHUMP00000019862; VCL; VINC; VINC_HUMAN; Vinculin;



Metavinculin is muscle-specific.

Vinculin binding sites have been identified on other cytoskeletal proteins, including Talin and α-actinin. In addition, vinculin, Talin and α-actinin each contain Actin binding sites. Expression of vinculin and Talin has been shown to be affected by the level of Actin expression.



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P18206 As Substrate

Site PTM Type Enzyme
T8 Phosphorylation
S52 Phosphorylation
K59 Ubiquitination
K71 Acetylation
K71 Ubiquitination
C85 S-Nitrosylation
S97 Phosphorylation
Y100 Phosphorylation P12931 (SRC)
S101 Phosphorylation
Y107 Phosphorylation
S112 Phosphorylation
K173 Acetylation
S207 Phosphorylation
K216 Ubiquitination
K219 Ubiquitination
K228 Ubiquitination
S252 Phosphorylation
S260 Phosphorylation
S272 Phosphorylation
S275 Phosphorylation
K276 Acetylation
S288 Phosphorylation
S290 Phosphorylation
K308 Ubiquitination
K316 Ubiquitination
T324 Phosphorylation
S345 Phosphorylation
S346 Phosphorylation
S357 Phosphorylation
K366 Ubiquitination
T378 Phosphorylation
S380 Phosphorylation
S383 Phosphorylation
K386 Ubiquitination
K387 Ubiquitination
R409 Methylation
K426 Ubiquitination
S434 Phosphorylation
S439 Phosphorylation
T442 Phosphorylation
S443 Phosphorylation
K444 Acetylation
K444 Ubiquitination
K464 Ubiquitination
K476 Ubiquitination
K496 Acetylation
T508 Phosphorylation
R512 Methylation
Y537 Phosphorylation
K544 Ubiquitination
C545 S-Nitrosylation
S566 Phosphorylation
S574 Phosphorylation
S579 Phosphorylation
K581 Ubiquitination
K584 Ubiquitination
S596 Phosphorylation
S600 Phosphorylation
T604 Phosphorylation
T614 Phosphorylation
R622 Methylation
S637 Phosphorylation
K639 Ubiquitination
T643 Phosphorylation
K655 Ubiquitination
T657 Phosphorylation
S664 Phosphorylation
K666 Ubiquitination
T672 Phosphorylation
S677 Phosphorylation
Y692 Phosphorylation
T697 Phosphorylation
K699 Acetylation
K699 Ubiquitination
K708 Ubiquitination
T719 Phosphorylation
K720 Ubiquitination
S721 Phosphorylation
S726 Phosphorylation
K731 Ubiquitination
T754 Phosphorylation
S755 Phosphorylation
K768 Acetylation
K768 Ubiquitination
K778 Ubiquitination
K784 Ubiquitination
S787 Phosphorylation
K792 Ubiquitination
S795 Phosphorylation
K802 Ubiquitination
S809 Phosphorylation
K815 Ubiquitination
S816 Phosphorylation
S820 Phosphorylation
Y822 Phosphorylation
K862 Ubiquitination
S972 Phosphorylation
S981 Phosphorylation
S982 Phosphorylation
K983 Ubiquitination
K992 Acetylation
R993 Methylation
S1002 Phosphorylation
R1003 Methylation
K1020 Ubiquitination
C1053 S-Nitrosylation
K1064 Ubiquitination
K1070 Acetylation
K1070 Ubiquitination
S1080 Phosphorylation
S1101 Phosphorylation
S1113 Phosphorylation
T1123 Phosphorylation
T1130 Phosphorylation
Y1133 Phosphorylation P12931 (SRC)

Research Backgrounds


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.


Phosphorylated; 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 (By similarity).

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

Subcellular Location:

Cell membrane>Peripheral membrane protein>Cytoplasmic side. Cell junction>Adherens junction. Cell junction>Focal adhesion. Cytoplasm>Cytoskeleton. Cell membrane>Sarcolemma>Peripheral membrane protein>Cytoplasmic side.
Note: 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.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Metavinculin is muscle-specific.

Subunit Structure:

Exhibits self-association properties. Interacts with APBB1IP and NRAP (By similarity). Interacts with TLN1. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin (By similarity). Interacts with SYNM. Interacts with SORBS1 (By similarity). Interacts with CTNNA1. Binds to ACTN4; this interaction triggers conformational changes.


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 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. In isoform 2 (metavinculin) a 68 residue insertion in the tail domain promotes actin severing instead of bundling. 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.

Belongs to the vinculin/alpha-catenin family.

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Adherens junction.   (View pathway)

· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Bacterial invasion of epithelial cells.

· Human Diseases > Infectious diseases: Bacterial > Shigellosis.

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Organismal Systems > Immune system > Leukocyte transendothelial migration.   (View pathway)

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