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Catenin alpha-2 (Alpha N-catenin) (Alpha-catenin-related protein)

 CTNA2_HUMAN             Reviewed;         953 AA.
P26232; B3KXE5; B7Z2W7; B7Z352; B7Z898; Q4ZFW1; Q53R26; Q53R33;
Q53T67; Q53T71; Q53TM8; Q7Z3L1; Q7Z3Y0;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
20-JUN-2018, entry version 172.
RecName: Full=Catenin alpha-2;
AltName: Full=Alpha N-catenin;
AltName: Full=Alpha-catenin-related protein;
Name=CTNNA2; Synonyms=CAPR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8432524; DOI=10.1006/geno.1993.1004;
Claverie J.-M., Hardelin J.-P., Legouis R., Levilliers J.,
Bougueleret L., Mattei M.-G., Petit C.;
"Characterization and chromosomal assignment of a human cDNA encoding
a protein related to the murine 102-kDa cadherin-associated protein
(alpha-catenin).";
Genomics 15:13-20(1993).
[2]
SEQUENCE REVISION TO C-TERMINUS.
Hardelin J.-P.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
TISSUE=Brain, Hippocampus, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Hippocampus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=PNS;
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).
[8]
INTERACTION WITH ZNF639, AND SUBCELLULAR LOCATION.
PubMed=16182284; DOI=10.1016/j.yexcr.2005.06.018;
Bogaerts S., Vanlandschoot A., van Hengel J., van Roy F.;
"Nuclear translocation of alphaN-catenin by the novel zinc finger
transcriptional repressor ZASC1.";
Exp. Cell Res. 311:1-13(2005).
[9]
ALTERNATIVE SPLICING (ISOFORM 6).
PubMed=18163523; DOI=10.1002/ajmg.b.30679;
Mexal S., Berger R., Pearce L., Barton A., Logel J., Adams C.E.,
Ross R.G., Freedman R., Leonard S.;
"Regulation of a novel alphaN-catenin splice variant in schizophrenic
smokers.";
Am. J. Med. Genet. B Neuropsychiatr. Genet. 147:759-768(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
-!- 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:0000250|UniProtKB:Q61301}.
-!- SUBUNIT: Interacts with CDH1 and CDH2 (By similarity). Interacts
with ZNF639; recruits CTNNA2 to the nucleus (PubMed:16182284).
{ECO:0000250|UniProtKB:P30997, ECO:0000269|PubMed:16182284}.
-!- INTERACTION:
Q9UID6:ZNF639; NbExp=7; IntAct=EBI-3953920, EBI-947476;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q61301}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q61301}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q61301}. Cytoplasm
{ECO:0000269|PubMed:16182284}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q61301}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:Q61301}. Cell projection, axon
{ECO:0000250|UniProtKB:Q61301}. Nucleus
{ECO:0000269|PubMed:16182284}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=AlphaN-catenin II;
IsoId=P26232-1; Sequence=Displayed;
Name=2; Synonyms=AlphaN-catenin I;
IsoId=P26232-2; Sequence=VSP_020337;
Name=3;
IsoId=P26232-3; Sequence=VSP_038009;
Note=No experimental confirmation available.;
Name=4;
IsoId=P26232-4; Sequence=VSP_038008, VSP_020337;
Name=5;
IsoId=P26232-5; Sequence=VSP_038007, VSP_020337;
Note=No experimental confirmation available.;
Name=6; Synonyms=AlphaN-catenin III;
IsoId=P26232-6; Sequence=VSP_038005, VSP_038006, VSP_020337;
-!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
{ECO:0000305}.
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EMBL; M94151; AAA58407.2; -; mRNA.
EMBL; AK127226; BAG54457.1; -; mRNA.
EMBL; AK295181; BAH12003.1; -; mRNA.
EMBL; AK295493; BAH12088.1; -; mRNA.
EMBL; AK303035; BAH13884.1; -; mRNA.
EMBL; BX537769; CAD97832.1; -; mRNA.
EMBL; AC008067; AAY15073.1; -; Genomic_DNA.
EMBL; AC010975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011741; AAX93241.1; -; Genomic_DNA.
EMBL; AC011746; AAY15008.1; -; Genomic_DNA.
EMBL; AC016670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC016716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC096573; AAY14758.1; -; Genomic_DNA.
EMBL; AC096753; AAY14763.1; -; Genomic_DNA.
EMBL; AC104780; AAX88946.1; -; Genomic_DNA.
EMBL; FJ695201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471053; EAW99564.1; -; Genomic_DNA.
EMBL; CH471053; EAW99565.1; -; Genomic_DNA.
EMBL; BC052996; AAH52996.1; -; mRNA.
CCDS; CCDS42703.2; -. [P26232-2]
CCDS; CCDS54371.1; -. [P26232-3]
CCDS; CCDS62944.1; -. [P26232-1]
CCDS; CCDS62945.1; -. [P26232-6]
CCDS; CCDS74531.1; -. [P26232-4]
PIR; A45011; A45011.
RefSeq; NP_001158355.1; NM_001164883.1. [P26232-3]
RefSeq; NP_001269526.1; NM_001282597.2. [P26232-1]
RefSeq; NP_001269527.1; NM_001282598.1. [P26232-5]
RefSeq; NP_001269528.1; NM_001282599.1. [P26232-6]
RefSeq; NP_001269529.1; NM_001282600.1. [P26232-4]
RefSeq; NP_001307739.1; NM_001320810.1.
RefSeq; NP_004380.2; NM_004389.3. [P26232-2]
RefSeq; XP_011530857.1; XM_011532555.2. [P26232-1]
RefSeq; XP_011530858.1; XM_011532556.2. [P26232-1]
RefSeq; XP_016858892.1; XM_017003403.1. [P26232-2]
UniGene; Hs.167368; -.
ProteinModelPortal; P26232; -.
SMR; P26232; -.
BioGrid; 107877; 28.
DIP; DIP-60979N; -.
IntAct; P26232; 8.
iPTMnet; P26232; -.
PhosphoSitePlus; P26232; -.
SwissPalm; P26232; -.
BioMuta; CTNNA2; -.
DMDM; 114152793; -.
EPD; P26232; -.
MaxQB; P26232; -.
PeptideAtlas; P26232; -.
PRIDE; P26232; -.
ProteomicsDB; 54314; -.
ProteomicsDB; 54315; -. [P26232-2]
ProteomicsDB; 54316; -. [P26232-3]
ProteomicsDB; 54317; -. [P26232-4]
ProteomicsDB; 54318; -. [P26232-5]
ProteomicsDB; 54319; -. [P26232-6]
TopDownProteomics; P26232-6; -. [P26232-6]
Ensembl; ENST00000343114; ENSP00000341500; ENSG00000066032. [P26232-6]
Ensembl; ENST00000402739; ENSP00000384638; ENSG00000066032. [P26232-1]
Ensembl; ENST00000466387; ENSP00000418191; ENSG00000066032. [P26232-2]
Ensembl; ENST00000496558; ENSP00000419295; ENSG00000066032. [P26232-2]
Ensembl; ENST00000541047; ENSP00000444675; ENSG00000066032. [P26232-4]
Ensembl; ENST00000629316; ENSP00000486160; ENSG00000066032. [P26232-3]
GeneID; 1496; -.
KEGG; hsa:1496; -.
UCSC; uc010yse.3; human. [P26232-1]
CTD; 1496; -.
DisGeNET; 1496; -.
EuPathDB; HostDB:ENSG00000066032.18; -.
GeneCards; CTNNA2; -.
HGNC; HGNC:2510; CTNNA2.
HPA; CAB037175; -.
MIM; 114025; gene.
neXtProt; NX_P26232; -.
OpenTargets; ENSG00000066032; -.
PharmGKB; PA27013; -.
GeneTree; ENSGT00550000074411; -.
HOVERGEN; HBG000069; -.
InParanoid; P26232; -.
KO; K05691; -.
OMA; WENQVRI; -.
OrthoDB; EOG091G01KR; -.
PhylomeDB; P26232; -.
TreeFam; TF313686; -.
Reactome; R-HSA-375170; CDO in myogenesis.
SIGNOR; P26232; -.
ChiTaRS; CTNNA2; human.
GenomeRNAi; 1496; -.
PRO; PR:P26232; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000066032; -.
CleanEx; HS_CTNNA2; -.
ExpressionAtlas; P26232; baseline and differential.
Genevisible; P26232; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0051015; F:actin filament binding; IEA:InterPro.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
GO; GO:0048854; P:brain morphogenesis; ISS:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0060134; P:prepulse inhibition; ISS:UniProtKB.
GO; GO:0021942; P:radial glia guided migration of Purkinje cell; ISS:UniProtKB.
GO; GO:0051823; P:regulation of synapse structural plasticity; ISS: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;
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_0000064263.
MOD_RES 632 632 Phosphothreonine.
{ECO:0000250|UniProtKB:Q61301}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000250|UniProtKB:Q61301}.
MOD_RES 901 901 Phosphoserine.
{ECO:0000250|UniProtKB:Q61301}.
MOD_RES 939 939 Phosphoserine.
{ECO:0000250|UniProtKB:Q61301}.
VAR_SEQ 1 368 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038008.
VAR_SEQ 1 351 Missing (in isoform 6).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_038005.
VAR_SEQ 1 1 M -> MSGLICLQYGLWHGQKIDFGGPRRLLQRNRGEGSM
(in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038007.
VAR_SEQ 352 352 N -> MDGWRRPLQSVGKVCEKNMKTSEMHTMSGAQ (in
isoform 6).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_038006.
VAR_SEQ 766 858 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038009.
VAR_SEQ 811 858 Missing (in isoform 2, isoform 4, isoform
5 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_020337.
CONFLICT 122 122 T -> A (in Ref. 3; BAH12003).
{ECO:0000305}.
CONFLICT 182 182 E -> K (in Ref. 1; AAA58407).
{ECO:0000305}.
CONFLICT 309 309 S -> SS (in Ref. 5; AAY15008).
{ECO:0000305}.
CONFLICT 651 652 SR -> RG (in Ref. 1; AAA58407).
{ECO:0000305}.
SEQUENCE 953 AA; 105313 MW; 5FC88907B37E8A6C 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 IAGISNAAQA 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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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
18-272-197076 alpha Catenin - Rabbit polyclonal to alpha Catenin; Cadherin-associated protein; Alpha E-catenin; NY-REN-13 antigen Polyclonal 0.5 ml
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
20-272-192389 alpha T Catenin - Mouse monoclonal [892_24D2S] to alpha T Catenin; Alpha T-catenin; Cadherin-associated protein Monoclonal 0.1 mg
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
EIAAB09851 Alpha T-catenin,Cadherin-associated protein,Catenin alpha-3,CTNNA3,Homo sapiens,Human
EIAAB09852 Alpha T-catenin,Cadherin-associated protein,Catenin alpha-3,Catna3,Ctnna3,Mouse,Mus musculus
EIAAB09848 Alpha N-catenin,Catenin alpha-2,Chicken,CTNNA2,Gallus gallus,Neural alpha-catenin
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
18-272-195399 delta 2 Catenin - Rabbit polyclonal to delta 2 Catenin; Delta-catenin; Neural plakophilin-related ARM-repeat protein; NPRAP; Neurojungin; GT24 Polyclonal 0.1 ml
18-272-195400 delta 2 Catenin - Rabbit polyclonal to delta 2 Catenin; Delta-catenin; Neural plakophilin-related ARM-repeat protein; NPRAP; Neurojungin; GT24 Polyclonal 0.1 ml
E2614h Human Alpha Catenin Like Protein 1 ELISA Kit 96T


 

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