product summary
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company name :
MyBioSource
product type :
protein
product name :
Recombinant Human Vinculin
catalog :
MBS957842
quantity :
0.05 mg (E-Coli)
price :
165 USD
more info or order :
product information
catalog number :
MBS957842
products type :
Recombinant Protein
products full name :
Recombinant Human Vinculin
products short name :
Vinculin
products name syn :
Metavinculin; MV
other names :
vinculin isoform VCL; Vinculin; vinculin; vinculin; Metavinculin; MV
products gene name :
VCL
other gene names :
VCL; VCL; MV; MVCL; CMD1W; CMH15; HEL114; MV
uniprot entry name :
VINC_HUMAN
host :
E Coli
sequence positions :
2-235
sequence length :
1066
sequence :
PVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDL
TAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFI
KVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSG
TSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDL
VTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMN
TVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVE
purity :
Greater than 90% as determined by SDS-PAGE.
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
products categories :
Cell Adhesion
products description :
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.
products references :
Complete sequence of human vinculin and assignment of the gene to chromosome 10.Weller P.A., Ogryzko E.P., Corben E.B., Zhidkova N.I., Patel B., Price G.J., Spurr N.K., Koteliansky V.E., Critchley D.R.Proc. Natl. Acad. Sci. U.S.A. 87:5667-5671(1990) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) The DNA sequence and comparative analysis of human chromosome 10.Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.Nature 429:375-381(2004) Organization of the human gene encoding the cytoskeletal protein vinculin and the sequence of the vinculin promoter.Moiseyeva E.P., Weller P.A., Zhidkova N.I., Corben E.B., Patel B., Jasinska I., Koteliansky V.E., Critchley D.R.J. Biol. Chem. 268:4318-4325(1993) Lubec G., Chen W.-Q., Sun Y.Submitted (DEC-2008) to UniProtKB An additional exon in the human vinculin gene specifically encodes meta-vinculin-specific difference peptide. Cross-species comparison reveals variable and conserved motifs in the meta-vinculin insert.Koteliansky V.E., Ogryzko E.P., Zhidkova N.I., Weller P.A., Critchley D.R., Vancompernolle K., Vandekerckhove J., Strasser P., Way M., Gimona M., Small J.V.Eur. J. Biochem. 204:767-772(1992) Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.Nat. Biotechnol. 21:566-569(2003) The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading.Zhang Z., Izaguirre G., Lin S.-Y., Lee H.Y., Schaefer E., Haimovich B.Mol. Biol. Cell 15:4234-4247(2004) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) Human alpha-synemin interacts directly with vinculin and metavinculin.Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.Biochem. J. 409:657-667(2008) Cell cycle regulated phosphorylation of LIMD1 in cell lines and expression in human breast cancers.Huggins C.J., Andrulis I.L.Cancer Lett. 267:55-66(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Vinculin is a dually regulated actin filament barbed end-capping and side-binding protein.Le Clainche C., Dwivedi S.P., Didry D., Carlier M.F.J. Biol. Chem. 285:23420-23432(2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) The C-terminal tail domain of metavinculin, vinculin's splice variant, severs actin filaments.Janssen M.E., Liu H., Volkmann N., Hanein D.J. Cell Biol. 197:585-593(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structural basis for amplifying vinculin activation by talin.Izard T., Vonrhein C.J. Biol. Chem. 279:27667-27678(2004) Vinculin activation by talin through helical bundle conversion.Izard T., Evans G., Borgon R.A., Rush C.L., Bricogne G., Bois P.R.J.Nature 427:171-175(2004) Metavinculin mutations alter actin interaction in dilated cardiomyopathy.Olson T.M., Illenberger S., Kishimoto N.Y., Huttelmaier S., Keating M.T., Jockusch B.M.Circulation 105:431-437(2002) Identification of a metavinculin missense mutation, R975W, associated with both hypertrophic and dilated cardiomyopathy.Vasile V.C., Will M.L., Ommen S.R., Edwards W.D., Olson T.M., Ackerman M.J.Mol. Genet. Metab. 87:169-174(2006) A missense mutation in a ubiquitously expressed protein, vinculin, confers susceptibility to hypertrophic cardiomyopathy.Vasile V.C., Ommen S.R., Edwards W.D., Ackerman M.J.Biochem. Biophys. Res. Commun. 345:998-1003(2006)
ncbi gi num :
4507877
ncbi acc num :
NP_003364.1
ncbi gb acc num :
NM_003373.3
uniprot acc num :
P18206
ncbi mol weight :
53.4kD
ncbi pathways :
ARMS-mediated Activation Pathway (1269471); Adherens Junction Pathway (83070); Adherens Junction Pathway (481); Amoebiasis Pathway (167324); Amoebiasis Pathway (167191); Axon Guidance Pathway (1270303); Bacterial Invasion Of Epithelial Cells Pathway (149807); Bacterial Invasion Of Epithelial Cells Pathway (148661); Cytokine Signaling In Immune System Pathway (1269310); DAP12 Interactions Pathway (1269283)
ncbi summary :
Vinculin is a cytoskeletal protein associated with cell-cell and cell-matrix junctions, where it is thought to function as one of several interacting proteins involved in anchoring F-actin to the membrane. Defects in VCL are the cause of cardiomyopathy dilated type 1W. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in 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. [provided by RefSeq, Jul 2008]
uniprot summary :
Vinculin: 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. Exhibits self-association properties. Interacts with NRAP and SORBS1. Interacts with TLN1. Interacts with SYNM. 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. Metavinculin is muscle-specific. Belongs to the vinculin/alpha-catenin family. 3 isoforms of the human protein are produced by alternative splicing. Protein type: Cell adhesion; Motility/polarity/chemotaxis; Cytoskeletal. Chromosomal Location of Human Ortholog: 10q22.2. Cellular Component: actin cytoskeleton; adherens junction; brush border; cell; cell-cell adherens junction; cell-matrix junction; costamere; cytoskeleton; cytosol; extracellular region; fascia adherens; focal adhesion; intercellular junction; lipid raft; plasma membrane; protein complex; zonula adherens. Molecular Function: actin binding; alpha-catenin binding; beta-catenin binding; cadherin binding; protein binding; structural molecule activity; ubiquitin protein ligase binding. Biological Process: apical junction assembly; axon extension; blood coagulation; cell adhesion; cell motility; cell-matrix adhesion; lamellipodium biogenesis; morphogenesis of an epithelium; muscle contraction; negative regulation of cell migration; platelet activation; platelet degranulation. Disease: Cardiomyopathy, Dilated, 1w
size1 :
0.05 mg (E-Coli)
price1 :
165 USD
size2 :
0.2 mg (E-Coli)
price2 :
275
size3 :
0.5 mg (E-Coli)
price3 :
515
size4 :
1 mg (E-Coli)
price4 :
755
more info or order :
company information
MyBioSource
P.O. Box 153308
San Diego, CA 92195-3308
sales@mybiosource.com
https://www.mybiosource.com
1-888-627-0165
headquarters: USA
MyBioSource, LLC was orginally founded in Vancouver by three enthusiastic scientists who are passionate about providing the world with the best reagents available. Together, they form a company with a big vision known as MyBioSource. MyBioSource is now located in San Diego, California, USA.

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