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Catenin alpha-2 (Alpha N-catenin)

 CTNA2_MOUSE             Reviewed;         953 AA.
Q61301; Q3TY37; Q61300; Q6AXD1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 155.
RecName: Full=Catenin alpha-2;
AltName: Full=Alpha N-catenin;
Name=Ctnna2; Synonyms=Catna2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=8174789; DOI=10.1006/dbio.1994.1124;
Uchida N., Shimamura K., Miyatani S., Copeland N.G., Gilbert D.J.,
Jenkins N.A., Takeichi M.;
"Mouse alpha N-catenin: two isoforms, specific expression in the
nervous system, and chromosomal localization of the gene.";
Dev. Biol. 163:75-85(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Visual cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=12089526; DOI=10.1038/ng908;
Park C., Falls W., Finger J.H., Longo-Guess C.M., Ackerman S.L.;
"Deletion in Catna2, encoding alpha N-catenin, causes cerebellar and
hippocampal lamination defects and impaired startle modulation.";
Nat. Genet. 31:279-284(2002).
[5]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12123610; DOI=10.1016/S0896-6273(02)00748-1;
Togashi H., Abe K., Mizoguchi A., Takaoka K., Chisaka O., Takeichi M.;
"Cadherin regulates dendritic spine morphogenesis.";
Neuron 35:77-89(2002).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-901, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[7]
DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15034585; DOI=10.1038/nn1212;
Abe K., Chisaka O., Van Roy F., Takeichi M.;
"Stability of dendritic spines and synaptic contacts is controlled by
alpha N-catenin.";
Nat. Neurosci. 7:357-363(2004).
[8]
DEVELOPMENTAL STAGE.
PubMed=16185771; DOI=10.1016/j.devbrainres.2005.08.004;
Ajioka I., Nakajima K.;
"Switching of alpha-catenin from alphaE-catenin in the cortical
ventricular zone to alphaN-catenin II in the intermediate zone.";
Brain Res. Dev. Brain Res. 160:106-111(2005).
[9]
DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
PubMed=16457793; DOI=10.1016/j.brainres.2005.12.057;
Stocker A.M., Chenn A.;
"Differential expression of alpha-E-catenin and alpha-N-catenin in the
developing cerebral cortex.";
Brain Res. 1073:151-158(2006).
[10]
DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=16691566; DOI=10.1002/dvdy.20841;
Uemura M., Takeichi M.;
"Alpha N-catenin deficiency causes defects in axon migration and
nuclear organization in restricted regions of the mouse brain.";
Dev. Dyn. 235:2559-2566(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632; SER-640; SER-651;
SER-901 AND SER-939, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May function as a linker between cadherin adhesion
receptors and the cytoskeleton to regulate cell-cell adhesion and
differentiation in the nervous system. Regulates morphological
plasticity of synapses and cerebellar and hippocampal lamination
during development. Functions in the control of startle
modulation. {ECO:0000269|PubMed:12089526,
ECO:0000269|PubMed:12123610, ECO:0000269|PubMed:15034585}.
-!- SUBUNIT: Interacts with CDH1 and CDH2 (By similarity). Interacts
with ZNF639; recruits CTNNA2 to the nucleus (By similarity).
{ECO:0000250|UniProtKB:P26232, ECO:0000250|UniProtKB:P30997}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-774089, EBI-774089;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16457793};
Peripheral membrane protein {ECO:0000305|PubMed:16457793};
Cytoplasmic side {ECO:0000305|PubMed:16457793}. Cytoplasm
{ECO:0000269|PubMed:16457793}. Cytoplasm, cytoskeleton
{ECO:0000305|PubMed:15034585}. Cell junction, adherens junction
{ECO:0000269|PubMed:16457793, ECO:0000269|PubMed:16691566}. Cell
projection, axon {ECO:0000269|PubMed:16457793,
ECO:0000269|PubMed:16691566}. Nucleus
{ECO:0000250|UniProtKB:P26232}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=alpha N-catenin II;
IsoId=Q61301-1; Sequence=Displayed;
Name=2; Synonyms=alpha N-catenin I;
IsoId=Q61301-2; Sequence=VSP_006734;
Name=3;
IsoId=Q61301-3; Sequence=VSP_038010, VSP_006734;
-!- TISSUE SPECIFICITY: Expressed almost exclusively in the nervous
system. {ECO:0000269|PubMed:8174789}.
-!- DEVELOPMENTAL STAGE: The ratio of the two isoforms changes during
development; isoform 1 is more abundant than isoform 2 in earlier
embryonic stages, whereas isoform 2 is predominant in the adult
stage. Expressed in the ventricular zone and in neurons of the
developing cortical plate (at protein level). Expressed in
migrating neurons of the external granule cell layer at E13.5
while expression appears in the Purkinje cell layer at E17.5 (at
protein level). Expressed postnatally in Purkinje cells and
hippocampus (at protein level). {ECO:0000269|PubMed:12089526,
ECO:0000269|PubMed:16185771, ECO:0000269|PubMed:16457793,
ECO:0000269|PubMed:8174789}.
-!- DISRUPTION PHENOTYPE: Mice generally die within 24 hours after
birth. They display altered Purkinje cells migration, unstable
synaptic junctions, defective ventricular architecture, impaired
axon migration, reduced number of neurons in specific nuclei, and
disordered laminar formation. {ECO:0000269|PubMed:12089526,
ECO:0000269|PubMed:12123610, ECO:0000269|PubMed:15034585,
ECO:0000269|PubMed:16691566}.
-!- MISCELLANEOUS: The cdf (cerebellar deficient folia) mice are
viable but are ataxic and have cerebellar hypoplasia associated
with abnormal lobulation of the cerebellum. They also display
defects in Purkinje cells positioning and in packing density and
lamination. Fear conditioning and prepulse inhibition of the
startle response are altered in cdf mice. Those phenotypes are
associated with alteration of the Ctnna2 gene which results in the
C-terminal truncation of the protein and are rescued by expression
of a Ctnna2 transgene (isoform 2).
-!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
{ECO:0000305}.
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EMBL; D25282; BAA04970.1; -; mRNA.
EMBL; D25281; BAA04969.1; -; mRNA.
EMBL; AK158916; BAE34726.1; -; mRNA.
EMBL; BC079648; AAH79648.1; -; mRNA.
CCDS; CCDS20250.1; -. [Q61301-1]
CCDS; CCDS39521.1; -. [Q61301-2]
PIR; I49499; I49499.
PIR; I49500; I49500.
RefSeq; NP_001103234.1; NM_001109764.1. [Q61301-1]
RefSeq; NP_033949.2; NM_009819.2. [Q61301-1]
RefSeq; NP_663785.2; NM_145732.2. [Q61301-2]
RefSeq; XP_011239496.1; XM_011241194.2. [Q61301-3]
RefSeq; XP_017176861.1; XM_017321372.1.
UniGene; Mm.34637; -.
PDB; 4K1O; X-ray; 2.60 A; A=651-953.
PDB; 4ONS; X-ray; 2.80 A; A/C=18-264.
PDB; 4P9T; X-ray; 2.50 A; A/B/C/D=13-261.
PDB; 5XFL; X-ray; 2.45 A; A/B/C/D=260-632.
PDBsum; 4K1O; -.
PDBsum; 4ONS; -.
PDBsum; 4P9T; -.
PDBsum; 5XFL; -.
ProteinModelPortal; Q61301; -.
SMR; Q61301; -.
BioGrid; 198511; 6.
DIP; DIP-31971N; -.
IntAct; Q61301; 6.
MINT; Q61301; -.
STRING; 10090.ENSMUSP00000124376; -.
iPTMnet; Q61301; -.
PhosphoSitePlus; Q61301; -.
SwissPalm; Q61301; -.
PaxDb; Q61301; -.
PeptideAtlas; Q61301; -.
PRIDE; Q61301; -.
Ensembl; ENSMUST00000075340; ENSMUSP00000074809; ENSMUSG00000063063. [Q61301-2]
Ensembl; ENSMUST00000159626; ENSMUSP00000124376; ENSMUSG00000063063. [Q61301-1]
Ensembl; ENSMUST00000161846; ENSMUSP00000123714; ENSMUSG00000063063. [Q61301-3]
GeneID; 12386; -.
KEGG; mmu:12386; -.
UCSC; uc009cjq.2; mouse. [Q61301-1]
UCSC; uc012enl.1; mouse. [Q61301-2]
CTD; 1496; -.
MGI; MGI:88275; Ctnna2.
eggNOG; KOG3681; Eukaryota.
eggNOG; ENOG410XSRU; LUCA.
GeneTree; ENSGT00550000074411; -.
HOGENOM; HOG000280724; -.
HOVERGEN; HBG000069; -.
InParanoid; Q61301; -.
KO; K05691; -.
PhylomeDB; Q61301; -.
TreeFam; TF313686; -.
Reactome; R-MMU-375170; CDO in myogenesis.
ChiTaRS; Ctnna2; mouse.
PRO; PR:Q61301; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000063063; Expressed in 110 organ(s), highest expression level in cerebral cortex.
CleanEx; MM_CTNNA2; -.
ExpressionAtlas; Q61301; baseline and differential.
GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0030424; C:axon; IMP:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0051015; F:actin filament binding; IEA:InterPro.
GO; GO:0045296; F:cadherin binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0007409; P:axonogenesis; IMP:UniProtKB.
GO; GO:0048854; P:brain morphogenesis; IMP:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
GO; GO:0048813; P:dendrite morphogenesis; IMP:UniProtKB.
GO; GO:0060134; P:prepulse inhibition; IMP:UniProtKB.
GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:UniProtKB.
GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:UniProtKB.
InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
InterPro; IPR001033; Alpha_catenin.
InterPro; IPR030046; CTNNA2.
InterPro; IPR006077; Vinculin/catenin.
InterPro; IPR000633; Vinculin_CS.
PANTHER; PTHR18914; PTHR18914; 1.
PANTHER; PTHR18914:SF23; PTHR18914:SF23; 1.
Pfam; PF01044; Vinculin; 2.
PRINTS; PR00805; ALPHACATENIN.
SUPFAM; SSF47220; SSF47220; 5.
PROSITE; PS00663; VINCULIN_1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Cytoskeleton; Developmental protein; Differentiation; Membrane;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 953 Catenin alpha-2.
/FTId=PRO_0000064264.
MOD_RES 632 632 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 901 901 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:21183079}.
MOD_RES 939 939 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 1 M -> MTDIHSSYTYTGSM (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038010.
VAR_SEQ 811 858 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:8174789}.
/FTId=VSP_006734.
CONFLICT 103 103 M -> K (in Ref. 1; BAA04970/BAA04969).
{ECO:0000305}.
CONFLICT 331 331 I -> M (in Ref. 1; BAA04970/BAA04969).
{ECO:0000305}.
CONFLICT 349 349 Y -> D (in Ref. 1; BAA04970/BAA04969).
{ECO:0000305}.
CONFLICT 558 558 M -> I (in Ref. 3; AAH79648).
{ECO:0000305}.
CONFLICT 618 618 D -> Y (in Ref. 1; BAA04970/BAA04969).
{ECO:0000305}.
CONFLICT 648 648 Missing (in Ref. 3; AAH79648).
{ECO:0000305}.
CONFLICT 660 660 D -> R (in Ref. 1; BAA04970/BAA04969).
{ECO:0000305}.
CONFLICT 817 817 F -> S (in Ref. 1; BAA04970).
{ECO:0000305}.
CONFLICT 862 862 A -> S (in Ref. 1; BAA04970/BAA04969).
{ECO:0000305}.
CONFLICT 911 911 P -> S (in Ref. 2; BAE34726).
{ECO:0000305}.
HELIX 22 39 {ECO:0000244|PDB:4P9T}.
HELIX 55 81 {ECO:0000244|PDB:4P9T}.
STRAND 83 85 {ECO:0000244|PDB:4P9T}.
HELIX 86 112 {ECO:0000244|PDB:4P9T}.
HELIX 117 165 {ECO:0000244|PDB:4P9T}.
HELIX 169 196 {ECO:0000244|PDB:4P9T}.
HELIX 200 229 {ECO:0000244|PDB:4P9T}.
HELIX 234 258 {ECO:0000244|PDB:4P9T}.
HELIX 275 286 {ECO:0000244|PDB:5XFL}.
STRAND 291 293 {ECO:0000244|PDB:5XFL}.
HELIX 296 319 {ECO:0000244|PDB:5XFL}.
HELIX 325 350 {ECO:0000244|PDB:5XFL}.
TURN 351 354 {ECO:0000244|PDB:5XFL}.
HELIX 360 391 {ECO:0000244|PDB:5XFL}.
HELIX 397 406 {ECO:0000244|PDB:5XFL}.
HELIX 411 437 {ECO:0000244|PDB:5XFL}.
HELIX 442 471 {ECO:0000244|PDB:5XFL}.
HELIX 476 502 {ECO:0000244|PDB:5XFL}.
HELIX 506 529 {ECO:0000244|PDB:5XFL}.
HELIX 533 558 {ECO:0000244|PDB:5XFL}.
HELIX 565 579 {ECO:0000244|PDB:5XFL}.
HELIX 581 597 {ECO:0000244|PDB:5XFL}.
HELIX 607 627 {ECO:0000244|PDB:5XFL}.
HELIX 668 673 {ECO:0000244|PDB:4K1O}.
HELIX 677 702 {ECO:0000244|PDB:4K1O}.
HELIX 710 729 {ECO:0000244|PDB:4K1O}.
HELIX 738 763 {ECO:0000244|PDB:4K1O}.
HELIX 769 791 {ECO:0000244|PDB:4K1O}.
STRAND 798 802 {ECO:0000244|PDB:4K1O}.
STRAND 805 809 {ECO:0000244|PDB:4K1O}.
HELIX 859 894 {ECO:0000244|PDB:4K1O}.
SEQUENCE 953 AA; 105286 MW; 52DC5230A4A4A159 CRC64;
MTSATSPIIL KWDPKSLEIR TLTVERLLEP LVTQVTTLVN TSNKGPSGKK KGRSKKAHVL
AASVEQATQN FLEKGEQIAK ESQDLKEELV AAVEDVRKQG ETMRIASSEF ADDPCSSVKR
GTMVRAARAL LSAVTRLLIL ADMADVMRLL SHLKIVEEAL EAVKNATNEQ DLANRFKEFG
KEMVKLNYVA ARRQQELKDP HCRDEMAAAR GALKKNATML YTASQAFLRH PDVAATRANR
DYVFKQVQEA IAGISSAAQA TSPTDEAKGH TGIGELAAAL NEFDNKIILD PMTFSEARFR
PSLEERLESI ISGAALMADS SCTRDDRRER IVAECNAVRQ ALQDLLSEYM NNTGRKEKGD
PLNIAIDKMT KKTRDLRRQL RKAVMDHISD SFLETNVPLL VLIEAAKSGN EKEVKEYAQV
FREHANKLVE VANLACSISN NEEGVKLVRM AATQIDSLCP QVINAALTLA ARPQSKVAQD
NMDVFKDQWE KQVRVLTEAV DDITSVDDFL SVSENHILED VNKCVIALQE GDVDTLDRTA
GAIRGRAARV IHIINAEMEN YEAGVYTEKV LEATKLLSET VMPRFAEQVE VAIEALSANV
PQPFEENEFI DASRLVYDGV RDIRKAVLMI RTPEELEDDS DFEQEDYDVR SRTSVQTEDD
QLIAGQSARA IMAQLPQEEK AKIAEQVEIF HQEKSKLDAE VAKWDDSGND IIVLAKQMCM
IMMEMTDFTR GKGPLKNTSD VINAAKKIAE AGSRMDKLAR AVADQCPDSA CKQDLLAYLQ
RIALYCHQLN ICSKVKAEVQ NLGGELIVSG TGVQSTFTTF YEVDCDVIDG GRASQLSTHL
PTCAEGAPIG SGSSDSSMLD SATSLIQAAK NLMNAVVLTV KASYVASTKY QKVYGTAAVN
SPVVSWKMKA PEKKPLVKRE KPEEFQTRVR RGSQKKHISP VQALSEFKAM DSF


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15-288-22833 Alpha-2 catenin - Alpha-catenin-related protein; Alpha N-catenin Polyclonal 0.1 mg
15-288-22833 Alpha-2 catenin - Alpha-catenin-related protein; Alpha N-catenin Polyclonal 0.05 mg
20-272-192389 alpha T Catenin - Mouse monoclonal [892_24D2S] to alpha T Catenin; Alpha T-catenin; Cadherin-associated protein Monoclonal 0.1 mg
20-272-191447 alpha Catenin - Mouse monoclonal [1G5] to alpha Catenin; Cadherin-associated protein; Alpha E-catenin; NY-REN-13 antigen Monoclonal 0.05 mg
18-272-195397 alpha 1 Catenin - Rabbit polyclonal to alpha 1 Catenin; Cadherin-associated protein; Alpha E-catenin; NY-REN-13 antigen Polyclonal 0.1 ml
18-272-197076 alpha Catenin - Rabbit polyclonal to alpha Catenin; Cadherin-associated protein; Alpha E-catenin; NY-REN-13 antigen Polyclonal 0.5 ml
EIAAB09848 Alpha N-catenin,Catenin alpha-2,Chicken,CTNNA2,Gallus gallus,Neural alpha-catenin
EIAAB09845 Alpha E-catenin,Cadherin-associated protein,Catenin alpha-1,CTNNA1,Homo sapiens,Human,Renal carcinoma antigen NY-REN-13
EIAAB09846 102 kDa cadherin-associated protein,Alpha E-catenin,CAP102,Catenin alpha-1,Catna1,Ctnna1,Mouse,Mus musculus
EIAAB09859 ACRP,Alpha-catenin-related protein,Alpha-catulin,Catenin alpha-like protein 1,CTNNAL1,Homo sapiens,Human
EIAAB09858 ACRP,Alpha-catenin-related protein,Alpha-catulin,Catenin alpha-like protein 1,Catnal1,Ctnnal1,Mouse,Mus musculus
EIAAB09852 Alpha T-catenin,Cadherin-associated protein,Catenin alpha-3,Catna3,Ctnna3,Mouse,Mus musculus
EIAAB09851 Alpha T-catenin,Cadherin-associated protein,Catenin alpha-3,CTNNA3,Homo sapiens,Human
15-288-22832 Alpha-1 catenin - Cadherin-associated protein; Alpha E-catenin; NY-REN-13 antigen Polyclonal 0.1 mg
15-288-22836 Alpha-1 catenin - Cadherin-associated protein; Alpha E-catenin; NY-REN-13 antigen Polyclonal 0.1 mg
15-288-22832 Alpha-1 catenin - Cadherin-associated protein; Alpha E-catenin; NY-REN-13 antigen Polyclonal 0.05 mg
15-288-22836 Alpha-1 catenin - Cadherin-associated protein; Alpha E-catenin; NY-REN-13 antigen Polyclonal 0.05 mg
EIAAB09849 Alpha N-catenin,Catenin alpha-2,Catna2,Ctnna2,Mouse,Mus musculus
MCA4410Z MOUSE ANTI HUMAN CATENIN ALPHA 3 Azide Free, Product Type Monoclonal Antibody, Specificity CATENIN, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applications WB, Clone 3 0.1 mg
RP 079-05 Alpha-Catenin; 0.5ml
Y058028 alpha T Catenin 100ul


 

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