Vinculin Antibody - #AF5122
(7)
(5)
| Product: | Vinculin Antibody |
| Catalog: | AF5122 |
| Description: | Rabbit polyclonal antibody to Vinculin |
| Application: | WB IHC |
| Cited expt.: | WB, IHC |
| Reactivity: | Human, Mouse, Rat |
| Prediction: | Pig, Bovine, Horse, Rabbit, Dog, Chicken |
| Mol.Wt.: | 130 kDa; 124kD(Calculated). |
| Uniprot: | P18206 |
| RRID: | AB_2837608 |
Related Downloads
Protocols
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
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.
Cite Format: Affinity Biosciences Cat# AF5122, RRID:AB_2837608.
Fold/Unfold
CMD1W; CMH15; Epididymis luminal protein 114; HEL114; Metavinculin; MV; MVCL; OTTHUMP00000019861; OTTHUMP00000019862; VCL; VINC; VINC_HUMAN; Vinculin;
Immunogens
A synthesized peptide derived from human Vinculin, corresponding to a region within N-terminal amino acids.
- P18206 VINC_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPSASPGDAGEQAIRQILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGSSPVAMQKAQQVSQGLDVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNGGPEGEEQIRGALAEARKIAELCDDPKERDDILRSLGEISALTSKLADLRRQGKGDSPEARALAKQVATALQNLQTKTNRAVANSRPAKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQDLLAKCDRVDQLTAQLADLAARGEGESPQARALASQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGKLGATAEKAAAVGTANKSTVEGIQASVKTARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEQLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKPGIPAAEVGIGVVAEADAADAAGFPVPPDMEDDYEPELLLMPSNQPVNQPILAAAQSLHREATKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ
Predictions
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.
High(score>80) Medium(80>score>50) Low(score<50) No confidence
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.
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.
Metavinculin is muscle-specific.
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)
References
Application: WB Species: Sample: RSCs
Application: IHC Species: Human Sample: gastric cancer specimens
Application: WB Species: human Sample: ESCC tissues
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