Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Uveal autoantigen with coiled-coil domains and ankyrin repeats (Nuclear membrane-binding protein) (Nucling)

 UACA_MOUSE              Reviewed;        1411 AA.
Q8CGB3; Q69ZG3; Q7TN77; Q8BJC8;
04-APR-2006, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 2.
23-MAY-2018, entry version 132.
RecName: Full=Uveal autoantigen with coiled-coil domains and ankyrin repeats;
AltName: Full=Nuclear membrane-binding protein;
Short=Nucling;
Name=Uaca; Synonyms=Kiaa1561;
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] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
STRAIN=129;
PubMed=12761289; DOI=10.1093/jb/mvg056;
Sakai T., Liu L., Shishido Y., Fukui K.;
"Identification of a novel, embryonal carcinoma cell-associated
molecule, nucling, that is up-regulated during cardiac muscle
differentiation.";
J. Biochem. 133:429-436(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Embryonic intestine;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-306.
STRAIN=C57BL/6J; TISSUE=Eye;
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).
[5]
FUNCTION, AND INTERACTION WITH APAF1.
PubMed=15271982; DOI=10.1074/jbc.M402902200;
Sakai T., Liu L., Teng X., Mukai-Sakai R., Shimada H., Kaji R.,
Mitani T., Matsumoto M., Toida K., Ishimura K., Shishido Y., Mak T.W.,
Fukui K.;
"Nucling recruits Apaf-1/pro-caspase-9 complex for the induction of
stress-induced apoptosis.";
J. Biol. Chem. 279:41131-41140(2004).
[6]
FUNCTION, INTERACTION WITH LGALS3, AND DISRUPTION PHENOTYPE.
PubMed=14961764; DOI=10.1042/BJ20031300;
Liu L., Sakai T., Sano N., Fukui K.;
"Nucling mediates apoptosis by inhibiting expression of galectin-3
through interference with nuclear factor kappaB signalling.";
Biochem. J. 380:31-41(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, 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).
[9]
FUNCTION, AND INTERACTION WITH RAB39A.
PubMed=23624502; DOI=10.1016/j.bbrc.2013.04.051;
Mori Y., Matsui T., Omote D., Fukuda M.;
"Small GTPase Rab39A interacts with UACA and regulates the retinoic
acid-induced neurite morphology of Neuro2A cells.";
Biochem. Biophys. Res. Commun. 435:113-119(2013).
-!- FUNCTION: Regulates APAF1 expression and plays an important role
in the regulation of stress-induced apoptosis. Promotes apoptosis
by regulating three pathways, apoptosome up-regulation,
LGALS3/galectin-3 down-regulation and NF-kappa-B inactivation.
Regulates the redistribution of APAF1 into the nucleus after
proapoptotic stress. Down-regulates the expression of LGALS3 by
inhibiting NFKB1. {ECO:0000269|PubMed:14961764,
ECO:0000269|PubMed:15271982}.
-!- FUNCTION: Modulates isoactin dynamics to regulate the
morphological alterations required for cell growth and motility.
Interaction with ARF6 may modulate cell shape and motility after
injury (By similarity). May be involved in multiple neurite
formation (PubMed:23624502). {ECO:0000250|UniProtKB:Q8HYY4,
ECO:0000269|PubMed:23624502}.
-!- SUBUNIT: Component of the apoptosome complex, composed of APAF1,
pro-caspase-9 and UACA. In the complex, it probably interacts
directly with APAF1. Interacts with LGALS3, ARF6 and ACTB.
Interacts with RAB39A. {ECO:0000269|PubMed:14961764,
ECO:0000269|PubMed:15271982, ECO:0000269|PubMed:23624502}.
-!- INTERACTION:
Q8BHD0:Rab39a; NbExp=3; IntAct=EBI-10767725, EBI-10767908;
Q8BHC1:Rab39b; NbExp=4; IntAct=EBI-10767725, EBI-10767682;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12761289}.
Cytoplasm {ECO:0000269|PubMed:12761289}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:12761289}. Note=Expressed diffusely in
cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8CGB3-1; Sequence=Displayed;
Name=2;
IsoId=Q8CGB3-2; Sequence=VSP_017874;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8CGB3-3; Sequence=VSP_017875;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in heart, liver, kidney and
testis. Weakly expressed in lung and skeletal muscle. Not
expressed in brain and spleen. {ECO:0000269|PubMed:12761289}.
-!- DEVELOPMENTAL STAGE: First detected at the E9.5 stage in heart at
the edge of both sides of the common ventricular chamber and is
then progressively increased and restricted to the myocardial wall
of left common ventricular chamber of heart.
{ECO:0000269|PubMed:12761289}.
-!- INDUCTION: Up-regulated during cardiomyogenic differentiation. By
apoptotic stress in a dose-dependent manner.
{ECO:0000269|PubMed:12761289}.
-!- DISRUPTION PHENOTYPE: Mice show a high incidence of inflammatory
lesions in preputial glands. Cells around the lesions showed
resistance to apoptosis. {ECO:0000269|PubMed:14961764}.
-!- SEQUENCE CAUTION:
Sequence=BAC78213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAD32481.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB030647; BAC78213.1; ALT_INIT; mRNA.
EMBL; AK173203; BAD32481.1; ALT_INIT; mRNA.
EMBL; BC042415; AAH42415.1; -; mRNA.
EMBL; AK087466; BAC39886.1; -; mRNA.
CCDS; CCDS23259.1; -. [Q8CGB3-3]
RefSeq; NP_082559.1; NM_028283.2.
RefSeq; XP_017169098.1; XM_017313609.1.
UniGene; Mm.68819; -.
ProteinModelPortal; Q8CGB3; -.
SMR; Q8CGB3; -.
BioGrid; 215442; 4.
IntAct; Q8CGB3; 5.
STRING; 10090.ENSMUSP00000062047; -.
iPTMnet; Q8CGB3; -.
PhosphoSitePlus; Q8CGB3; -.
PaxDb; Q8CGB3; -.
PeptideAtlas; Q8CGB3; -.
PRIDE; Q8CGB3; -.
GeneID; 72565; -.
KEGG; mmu:72565; -.
UCSC; uc009pzi.1; mouse. [Q8CGB3-3]
UCSC; uc009pzk.1; mouse. [Q8CGB3-1]
CTD; 55075; -.
MGI; MGI:1919815; Uaca.
eggNOG; ENOG410IJC6; Eukaryota.
eggNOG; COG0666; LUCA.
HOGENOM; HOG000147885; -.
HOVERGEN; HBG066395; -.
InParanoid; Q8CGB3; -.
PhylomeDB; Q8CGB3; -.
TreeFam; TF331274; -.
ChiTaRS; Uaca; mouse.
PRO; PR:Q8CGB3; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0043293; C:apoptosome; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005635; C:nuclear envelope; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:MGI.
GO; GO:0009411; P:response to UV; IMP:MGI.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR000727; T_SNARE_dom.
InterPro; IPR030227; UACA.
PANTHER; PTHR24173:SF23; PTHR24173:SF23; 3.
Pfam; PF12796; Ank_2; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 6.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS50192; T_SNARE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ANK repeat; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 1411 Uveal autoantigen with coiled-coil
domains and ankyrin repeats.
/FTId=PRO_0000231651.
REPEAT 69 98 ANK 1.
REPEAT 102 131 ANK 2.
REPEAT 135 164 ANK 3.
REPEAT 168 197 ANK 4.
REPEAT 201 230 ANK 5.
REPEAT 234 263 ANK 6.
COILED 299 379 {ECO:0000255}.
COILED 442 624 {ECO:0000255}.
COILED 652 1380 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9BZF9}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 398 Missing (in isoform 2).
{ECO:0000303|PubMed:15368895}.
/FTId=VSP_017874.
VAR_SEQ 264 264 G -> GGG (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017875.
CONFLICT 144 144 V -> A (in Ref. 3; AAH42415).
{ECO:0000305}.
CONFLICT 353 353 P -> L (in Ref. 3; AAH42415).
{ECO:0000305}.
CONFLICT 757 757 R -> K (in Ref. 3; AAH42415).
{ECO:0000305}.
CONFLICT 778 778 A -> T (in Ref. 3; AAH42415).
{ECO:0000305}.
SEQUENCE 1411 AA; 160813 MW; 0809D2DE9732F879 CRC64;
MKSLKSRLWK QDAPGPTSPS SPTAVASTQS AEWNKYDDRL MKAAERGDVE KVSSILAKKG
VHPGKLDVEG RSAFHVVASK GNLECLNAIL THGIDVATRD SAGRNALHLA AKYGHALCLQ
KLLQYNCPTE HVDLQGRTAL HDAVMADCPS SIQLLCDHGA SVNAKDIDGR TPLVLATQMC
RPTICQLLID RGADVNSRDK QNRTALMLGC EYGCRDAVEV LVKNGADLTL LDALGHDSSY
YARIGDNLDI LNLLKTASEN TNKGRELWRK GPPLQQRNLS HTQDEGSVKS TQREQREPHS
FQDLEIENED LREKLRKIQQ EQRILLDKVN GLQLQLNEEV MVADDLESER EKPKSLLAAK
EKQHEESLRT IEALKNRFKY FESDHPGPGS YPSNRKEDML HKQGQMYTTE PQCASPGIPP
HMHSRSMLRP LELSLPSQTS YSENEILKKE LETLRTYYDS AKQDRLKFQN ELAHKVAECK
ALALECERVK EDSDEQIKQL EDALKDVQKR MYESEGKVKQ MQTHFLALKE HLTNEAATGS
HRIIEELREQ LKDLKGKYEG ASAEVGKLRS QIKQSEMLVG EFKRDEGRLV EENKRLQKEC
GTCEVELERR GRRVVELEGQ LKELGAKLAL SVPTEKFESM KSSLSNDINE KVKRLAEVGR
DYESAQGEIR QLKRDLESVR AQHIRPEEHE QLRSRLEQKS GELGKKVSEL TLKNQTLQKD
VEKLHADNKL LNQQVHSLTV EMKTRYVPLR VSEEMKRSHD VNVEDLNKKL SEATQRYAEK
KQEAERLLAE NDKLTKNVSR LEAVFVAPEK HEKELMGLKS NIAELKKQLS ELNKKCGEGQ
EKIRALMSEN SSLKKTLSSQ YVPAKTHEEV KASLNSTVEK TNRALLEAKK RFDDTSQEVS
KLRDENEVLR RNLENVQNQM KADYVSLEEH SRRMSTVSQS LKEAQEANAA ILADHRQGQE
EIVSLHAEIK AQKKELDTIQ ECIKLKYAPL ARLEECERKF KATEKGLKEQ LSEQTHKCRQ
RDEEVKKGKQ ENERLRADLA ALQKELQDRN ALAEEAREAE RALSGKADEL SKQLKDLSQK
YSDVKSEREK LVEEKAKQAS EILAAQNLLQ KQPVPLEQVE ALKKSLNGTI EQLKEELRSK
QRCLEREQQT VSQLQQLLEN QKNSSVTLAE HLKLKEALEK EVGIMKASLR EKEEESQKKT
KEVSKLQTEV QTTKQALKNL ETREVVDMSK YKATKNDLET QISNLNDKLA SLNRKYDQAC
EEKVSAKDEK ELLHLSIEQE IRDQKERCDK SLTTIMELQQ RIQESAKQIE AKDNKITELL
NDVERLKQAL NGLSQLTYSS GSPTKRQSQL VDTLQQRVRD LQQQLADADR QHQEVIAIYR
THLLSAAQGH MDEDVQAALL QIIQMRQGLV C


Related products :

Catalog number Product name Quantity
EIAAB44766 Kiaa1561,Mouse,Mus musculus,Nuclear membrane-binding protein,Nucling,Uaca,Uveal autoantigen with coiled-coil domains and ankyrin repeats
EIAAB44768 Beta-actin-binding protein,BetaCAP73,Bos taurus,Bovine,UACA,Uveal autoantigen with coiled-coil domains and ankyrin repeats protein
EM768 Uveal autoantigen with coiled-coil domains and ankyrin repeats Elisa Kit 96T
EH2254 Uveal autoantigen with coiled-coil domains and ankyrin repeats Elisa Kit 96T
I1668 Uveal autoantigen with coiled-coil domains and ankyrin repeats (UACA), Dog, ELISA Kit 96T
CSB-EL025409DO Dog Uveal autoantigen with coiled-coil domains and ankyrin repeats(UACA) ELISA kit 96T
CSB-EL025409MO Mouse Uveal autoantigen with coiled-coil domains and ankyrin repeats(UACA) ELISA kit 96T
I1666 Uveal Autoantigen With Coiled Coil Domains And Ankyrin Repeats (UACA), Human, ELISA Kit 96T
CSB-EL025409BO Bovine Uveal autoantigen with coiled-coil domains and ankyrin repeats(UACA) ELISA kit 96T
E02A0075 Rat Anti Uveal autoantigen with coiled-coil domains and ankyrin repeats Antibodies ELISA 96T/kit
I1667 Uveal autoantigen with coiled-coil domains and ankyrin repeats (UACA), Bovine, ELISA Kit 96T
CSB-EL025409HU Human Uveal autoantigen with coiled-coil domains and ankyrin repeats(UACA) ELISA kit 96T
CSB-EL025409DO Dog Uveal autoantigen with coiled-coil domains and ankyrin repeats(UACA) ELISA kit SpeciesDog 96T
I1669 Uveal autoantigen with coiled-coil domains and ankyrin repeats (UACA), Human, ELISA Kit 96T
I1670 Uveal autoantigen with coiled-coil domains and ankyrin repeats (UACA), Mouse, ELISA Kit 96T
CSB-EL025409BO Bovine Uveal autoantigen with coiled-coil domains and ankyrin repeats(UACA) ELISA kit SpeciesBovine 96T
E12A0075 Chicken Anti Uveal autoantigen with coiled-coil domains and ankyrin repeats Antibodies ELISA 96T/kit
E11A0075 Bovine Anti Uveal autoantigen with coiled-coil domains and ankyrin repeats Antibodies ELISA 96T/kit
E01A0075 Human Anti Uveal autoantigen with coiled-coil domains and ankyrin repeats Antibodies ELISA 96T/kit
E09A0075 Monkey Anti Uveal autoantigen with coiled-coil domains and ankyrin repeats Antibodies ELISA 96T/kit
E04A0075 Rabbit Anti Uveal autoantigen with coiled-coil domains and ankyrin repeats Antibodies ELISA 96T/kit
E08A0075 Canine Anti Uveal autoantigen with coiled-coil domains and ankyrin repeats Antibodies ELISA 96T/kit
CSB-EL025409MO Mouse Uveal autoantigen with coiled-coil domains and ankyrin repeats(UACA) ELISA kit SpeciesMouse 96T
CSB-EL025409HU Human Uveal autoantigen with coiled-coil domains and ankyrin repeats(UACA) ELISA kit SpeciesHuman 96T
E03A0075 Mouse Anti Uveal autoantigen with coiled-coil domains and ankyrin repeats Antibodies ELISA 96T/kit


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur