Vinculin Recombinant Protein | VCL recombinant protein

Recombinant Human Vinculin

Cat. Num. AAA18464

• Gene Names: VCL; MV; MVCL; CMD1W; CMH15; HEL114
• Purity: Greater than 90% as determined by SDS-PAGE.
• Synonyms: Vinculin; N/A; Recombinant Human Vinculin; Metavinculin; MV; VCL recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater than 90% as determined by SDS-PAGE.
• Form/Format: Liquid or Lyophilized powder; If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8
• Sequence Positions: 2-235aa; Partial
• Sequence: PVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVE

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for VCL recombinant protein

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.

Product Categories/Family for VCL recombinant protein

Cell adhesion

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 and Uniprot Product Information

• NCBI GI #: 4507877
• NCBI GeneID: 7414
• NCBI Accession #: NP_003364.1
• NCBI GenBank Nucleotide #: NM_003373.3
• UniProt Accession #: P18206; Q16450; Q5SWX2; Q7Z3B8; Q8IXU7
• Molecular Weight: 53 kDa
• NCBI Official Full Name: vinculin isoform VCL
• NCBI Official Synonym Full Names: vinculin
• NCBI Official Symbol: VCL
• NCBI Official Synonym Symbols: MV; MVCL; CMD1W; CMH15; HEL114
• NCBI Protein Information: vinculin
• UniProt Protein Name: Vinculin
• UniProt Gene Name: VCL
• UniProt Synonym Gene Names: MV
• UniProt Entry Name: VINC_HUMAN