Description

  • Product name

    Recombinant Human Vinculin protein
    See all Vinculin proteins and peptides
  • Purity

    > 95 % SDS-PAGE.

  • Endotoxin level

    < 1.000 Eu/µg
  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAA VSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPY SVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEV VETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKE LLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTLEKMSAEINEIIRVLQL TSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPSASPGDAGEQAIR QILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGSSPVAM QKAQQVSQGLDVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNG GPEGEEQIRGALAEARKIAELCDDPKERDDILRSLGEISALTSKLADLRR QGKGDSPEARALAKQVATALQNLQTKTNRAVANSRPAKAAVHLEGKIEQA QRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQDLLAKCDRVDQ LTAQLADLAARGEGESPQARALASQLQDSLKDLKARMQEAMTQEVSDVFS DTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGKLGATAEKAAAV GTANKSTVEGIQASVKTARELTPQVVSAARILLRNPGNQAAYEHFETMKN QWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANIQPQMLV AGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMD AKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLE QLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMM AARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQC AKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILST VKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRT DAGFTLRWVRKTPWYQ
    • Predicted molecular weight

      117 kDa
    • Amino acids

      1 to 1066

Associated products

Specifications

Our Abpromise guarantee covers the use of ab151336 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

  • Form

    Lyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -80°C.

    pH: 7.20
    Constituents: 99% Phosphate Buffer, 0.88% Sodium chloride

  • Reconstitution
    Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 µg/ml. Dissolve the lyophilized protein in 1X PBS. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months..

General Info

  • Alternative names

    • CMD1W
    • CMH15
    • Epididymis luminal protein 114
    • HEL114
    • Metavinculin
    • MV
    • MVCL
    • OTTHUMP00000019861
    • OTTHUMP00000019862
    • VCL
    • VINC
    • VINC_HUMAN
    • Vinculin
    see all
  • Function

    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.
  • Tissue specificity

    Metavinculin is muscle-specific.
  • Involvement in disease

    Defects 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 similarities

    Belongs to the vinculin/alpha-catenin family.
  • Domain

    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. 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.
  • Post-translational
    modifications

    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.
    Aceylated; mainly by myristic acid but also small amount of palmitic acid.
  • Cellular localization

    Cytoplasm > 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

References

ab151336 has not yet been referenced specifically in any publications.

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