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

Centrosomal protein of 68 kDa (Cep68)

 CEP68_HUMAN             Reviewed;         757 AA.
Q76N32; B4DRQ1; D6W5F1; D6W5F2; O60326; Q9BQ18; Q9UDM9;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
25-OCT-2017, entry version 126.
RecName: Full=Centrosomal protein of 68 kDa;
Short=Cep68;
Name=CEP68; Synonyms=KIAA0582;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[2]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 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).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
SER-74.
TISSUE=Lymph;
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).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18042621; DOI=10.1242/jcs.020248;
Graser S., Stierhof Y.D., Nigg E.A.;
"Cep68 and Cep215 (Cdk5rap2) are required for centrosome cohesion.";
J. Cell Sci. 120:4321-4331(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
FUNCTION, INTERACTION WITH CNTLN AND NEK2, AND PHOSPHORYLATION.
PubMed=24554434; DOI=10.1242/jcs.139451;
Fang G., Zhang D., Yin H., Zheng L., Bi X., Yuan L.;
"Centlein mediates an interaction between C-Nap1 and Cep68 to maintain
centrosome cohesion.";
J. Cell Sci. 127:1631-1639(2014).
[12]
INTERACTION WITH BTRC, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
PROTEOLYTIC DEGRADATION.
PubMed=25704143; DOI=10.1016/j.ejcb.2015.01.004;
Man X., Megraw T.L., Lim Y.P.;
"Cep68 can be regulated by Nek2 and SCF complex.";
Eur. J. Cell Biol. 94:162-172(2015).
[13]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SCF(FBXW11) COMPLEX
AND BTRC, MUTAGENESIS OF 331-ASP--ASP-337; SER-332 AND ASP-337,
PHOSPHORYLATION AT SER-332, AND PROTEOLYTIC DEGRADATION.
PubMed=25503564; DOI=10.1038/ncb3076;
Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V.,
Florens L., Washburn M.P., Pagano M.;
"Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from
the PCM to allow centriole separation, disengagement and licensing.";
Nat. Cell Biol. 17:31-43(2015).
-!- FUNCTION: Involved in maintenance of centrosome cohesion, probably
as part of a linker structure which prevents centrosome splitting
(PubMed:18042621). Required for localization of CDK5RAP2 to the
centrosome during interphase (PubMed:24554434, PubMed:25503564).
{ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:24554434,
ECO:0000269|PubMed:25503564}.
-!- SUBUNIT: Interacts with CNTLN; the interaction recruits CEP68 to
the centrosome (PubMed:24554434). Interacts with the SCF(FBXW11)
complex which contains SKP1, CUL1 and FBXW11; the interaction is
probably mediated by FBXW11 and the complex also contains CDK5RAP2
and PCNT (PubMed:25503564). Also interacts with F-box protein BTRC
(PubMed:25704143, PubMed:25503564). Interacts with
serine/threonine-protein kinase PLK1; the interaction leads to
phosphorylation of CEP68 and its subsequent degradation
(PubMed:25503564). Interacts with NEK2; the interaction leads to
phosphorylation of CEP68 (PubMed:24554434).
{ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:24554434,
ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25704143}.
-!- INTERACTION:
Q9Y297:BTRC; NbExp=2; IntAct=EBI-9051024, EBI-307461;
Q96SN8:CDK5RAP2; NbExp=5; IntAct=EBI-9051024, EBI-308374;
Q13363-2:CTBP1; NbExp=3; IntAct=EBI-9051024, EBI-10171858;
O95613:PCNT; NbExp=3; IntAct=EBI-9051024, EBI-530012;
P53350:PLK1; NbExp=2; IntAct=EBI-9051024, EBI-476768;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-9051024, EBI-739895;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:14654843,
ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:25503564,
ECO:0000269|PubMed:25704143}. Note=Localizes to thin fibers
protruding away from the proximal ends of the two centrioles.
Dissociates from interphase centrosomes at the onset of mitosis.
{ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:25503564,
ECO:0000269|PubMed:25704143}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q76N32-1; Sequence=Displayed;
Name=2;
IsoId=Q76N32-2; Sequence=VSP_013476;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation by PLK1 is required for binding to BTRC in
prometaphase (PubMed:25503564). Phosphorylated directly or
indirectly by NEK2 (PubMed:24554434). NEK2-mediated
phosphorylation promotes CEP68 dissociation from the centrosome
and its degradation at the onset of mitosis (PubMed:25704143).
{ECO:0000269|PubMed:24554434, ECO:0000269|PubMed:25503564,
ECO:0000269|PubMed:25704143}.
-!- PTM: Ubiquitinated and targeted for proteasomal degradation in
early mitosis by the SCF(BTRC) and/or SCF(FBXW11) E3 ubiquitin-
protein ligase complexes (PubMed:25704143, PubMed:25503564).
Degradation is complete by prometaphase and is required for
removal of CDK5RAP2 from the peripheral pericentriolar material
and subsequent centriole separation (PubMed:25503564).
{ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25704143}.
-!- SEQUENCE CAUTION:
Sequence=BAA25508.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB011154; BAA25508.2; ALT_INIT; mRNA.
EMBL; AC007386; AAF03518.2; -; Genomic_DNA.
EMBL; AK299373; BAG61363.1; -; mRNA.
EMBL; CH471053; EAW99926.1; -; Genomic_DNA.
EMBL; CH471053; EAW99927.1; -; Genomic_DNA.
EMBL; CH471053; EAW99928.1; -; Genomic_DNA.
EMBL; CH471053; EAW99929.1; -; Genomic_DNA.
EMBL; BC002982; AAH02982.1; -; mRNA.
EMBL; BC004873; AAH04873.1; -; mRNA.
CCDS; CCDS1880.2; -. [Q76N32-1]
CCDS; CCDS82457.1; -. [Q76N32-2]
RefSeq; NP_001306029.1; NM_001319100.1. [Q76N32-1]
RefSeq; NP_001306030.1; NM_001319101.1. [Q76N32-2]
RefSeq; NP_055962.2; NM_015147.2. [Q76N32-1]
UniGene; Hs.709257; -.
ProteinModelPortal; Q76N32; -.
SMR; Q76N32; -.
BioGrid; 116789; 12.
DIP; DIP-57845N; -.
IntAct; Q76N32; 19.
MINT; MINT-7034577; -.
STRING; 9606.ENSP00000367229; -.
iPTMnet; Q76N32; -.
PhosphoSitePlus; Q76N32; -.
BioMuta; CEP68; -.
DMDM; 62899863; -.
EPD; Q76N32; -.
MaxQB; Q76N32; -.
PaxDb; Q76N32; -.
PeptideAtlas; Q76N32; -.
PRIDE; Q76N32; -.
Ensembl; ENST00000260569; ENSP00000260569; ENSG00000011523. [Q76N32-2]
Ensembl; ENST00000377990; ENSP00000367229; ENSG00000011523. [Q76N32-1]
GeneID; 23177; -.
KEGG; hsa:23177; -.
UCSC; uc002sdk.5; human. [Q76N32-1]
CTD; 23177; -.
DisGeNET; 23177; -.
EuPathDB; HostDB:ENSG00000011523.13; -.
GeneCards; CEP68; -.
HGNC; HGNC:29076; CEP68.
HPA; HPA040493; -.
HPA; HPA040620; -.
MIM; 616889; gene.
neXtProt; NX_Q76N32; -.
OpenTargets; ENSG00000011523; -.
PharmGKB; PA134991391; -.
eggNOG; ENOG410IIDK; Eukaryota.
eggNOG; ENOG41129RE; LUCA.
GeneTree; ENSGT00810000125473; -.
HOVERGEN; HBG050898; -.
InParanoid; Q76N32; -.
KO; K16764; -.
OMA; QAEYWAC; -.
OrthoDB; EOG091G0T7P; -.
PhylomeDB; Q76N32; -.
TreeFam; TF333570; -.
ChiTaRS; CEP68; human.
GeneWiki; CEP68; -.
GenomeRNAi; 23177; -.
PRO; PR:Q76N32; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000011523; -.
CleanEx; HS_CEP68; -.
ExpressionAtlas; Q76N32; baseline and differential.
Genevisible; Q76N32; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
GO; GO:0033365; P:protein localization to organelle; IMP:UniProtKB.
InterPro; IPR026696; AKAP6/CEP68.
PANTHER; PTHR14514; PTHR14514; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 757 Centrosomal protein of 68 kDa.
/FTId=PRO_0000089494.
COMPBIAS 532 537 Poly-Ser.
MOD_RES 332 332 Phosphoserine; by PLK1.
{ECO:0000269|PubMed:25503564}.
MOD_RES 472 472 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C0D9}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 492 628 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013476.
VARIANT 27 27 R -> G (in dbSNP:rs12611491).
/FTId=VAR_050794.
VARIANT 74 74 G -> S (in dbSNP:rs7572857).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_022363.
VARIANT 397 397 L -> P (in dbSNP:rs35501092).
/FTId=VAR_050795.
VARIANT 462 462 R -> C (in dbSNP:rs35694840).
/FTId=VAR_050796.
VARIANT 473 473 E -> Q (in dbSNP:rs35089924).
/FTId=VAR_050797.
MUTAGEN 331 337 Missing: Prevents binding to BTRC and
down-regulation of CEP68 during mitosis.
{ECO:0000269|PubMed:25503564}.
MUTAGEN 332 332 S->A: Prevents binding to BTRC and down-
regulation of CEP68 during mitosis.
{ECO:0000269|PubMed:25503564}.
MUTAGEN 337 337 D->A: Reduces CEP68 binding to BTRC.
{ECO:0000269|PubMed:12168954}.
SEQUENCE 757 AA; 81102 MW; 3FC969065CD5D2D7 CRC64;
MALGEEKAEA EASEDTKAQS YGRGSCRERE LDIPGPMSGE QPPRLEAEGG LISPVWGAEG
IPAPTCWIGT DPGGPSRAHQ PQASDANREP VAERSEPALS GLPPATMGSG DLLLSGESQV
EKTKLSSSEE FPQTLSLPRT TTICSGHDAD TEDDPSLADL PQALDLSQQP HSSGLSCLSQ
WKSVLSPGSA AQPSSCSISA SSTGSSLQGH QERAEPRGGS LAKVSSSLEP VVPQEPSSVV
GLGPRPQWSP QPVFSGGDAS GLGRRRLSFQ AEYWACVLPD SLPPSPDRHS PLWNPNKEYE
DLLDYTYPLR PGPQLPKHLD SRVPADPVLQ DSGVDLDSFS VSPASTLKSP TNVSPNCPPA
EATALPFSGP REPSLKQWPS RVPQKQGGMG LASWSQLAST PRAPGSRDAR WERREPALRG
AKDRLTIGKH LDMGSPQLRT RDRGWPSPRP EREKRTSQSA RRPTCTESRW KSEEEVESDD
EYLALPARLT QVSSLVSYLG SISTLVTLPT GDIKGQSPLE VSDSDGPASF PSSSSQSQLP
PGAALQGSGD PEGQNPCFLR SFVRAHDSAG EGSLGSSQAL GVSSGLLKTR PSLPARLDRW
PFSDPDVEGQ LPRKGGEQGK ESLVQCVKTF CCQLEELICW LYNVADVTDH GTAARSNLTS
LKSSLQLYRQ FKKDIDEHQS LTESVLQKGE ILLQCLLENT PVLEDVLGRI AKQSGELESH
ADRLYDSILA SLDMLAGCTL IPDKKPMAAM EHPCEGV


Related products :

Catalog number Product name Quantity
EIAAB06851 Centrosomal protein of 68 kDa,Cep68,CEP68,Homo sapiens,Human,KIAA0582
EIAAB06852 Centrosomal protein of 68 kDa,Cep68,Cep68,Mouse,Mus musculus
CEP68 CEP57 Gene centrosomal protein 57kDa
CSB-EL005246MO Mouse Centrosomal protein of 68 kDa(CEP68) ELISA kit 96T
CEP72 CEP68 Gene centrosomal protein 68kDa
201-20-1023 CEP68{centrosomal protein 68kDa}rabbit.pAb 0.1ml
CSB-EL005246HU Human Centrosomal protein of 68 kDa(CEP68) ELISA kit 96T
CSB-EL005246HU Human Centrosomal protein of 68 kDa(CEP68) ELISA kit SpeciesHuman 96T
CSB-EL005246MO Mouse Centrosomal protein of 68 kDa(CEP68) ELISA kit SpeciesMouse 96T
CEP68_MOUSE ELISA Kit FOR Centrosomal protein of 68 kDa; organism: Mouse; gene name: Cep68 96T
CEP68_HUMAN ELISA Kit FOR Centrosomal protein of 68 kDa; organism: Human; gene name: CEP68 96T
CSB-EL005246HU Human centrosomal protein 68kDa (CEP68) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL005246MO Mouse centrosomal protein 68kDa (CEP68) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
A4532 CEP68 Primary Antibody, CEP68, Species: Human Recombinant Protein Source: Rabbit Polyclonal 100ug
EIAAB08871 250 kDa centrosomal protein,Centrosomal Nek2-associated protein 1,Centrosomal protein 2,Centrosome-associated protein CEP250,Cep2,Cep250,Cep250,C-Nap1,Inmp,Intranuclear matrix protein,Mouse,Mus muscul
EIAAB08872 250 kDa centrosomal protein,Centrosomal Nek2-associated protein 1,Centrosomal protein 2,Centrosome-associated protein CEP250,CEP2,Cep250,CEP250,CNAP1,C-Nap1,Homo sapiens,Human
EIAAB06679 C6orf182,Centrosomal protein 57kDa-like protein 1,Centrosomal protein CEP57L1,Centrosomal protein of 57 kDa-related protein,CEP57L1,Cep57R,CEP57R,Cep57-related protein,Homo sapiens,Human
EIAAB06680 Centrosomal protein 57kDa-like protein 1,Centrosomal protein CEP57L1,Centrosomal protein of 57 kDa-related protein,Cep57l1,Cep57R,Cep57r,Cep57-related protein,Mouse,Mus musculus
EIAAB06681 Centrosomal protein 57kDa-like protein 1,Centrosomal protein CEP57L1,Centrosomal protein of 57 kDa-related protein,Cep57l1,Cep57R,Cep57r,Cep57-related protein,Rat,Rattus norvegicus
EIAAB08340 Centriolin,Centrosomal protein 1,Centrosomal protein of 110 kDa,CEP1,Cep110,CEP110,CNTRL,Homo sapiens,Human
EIAAB08339 Centriolin,Centrosomal protein 1,Centrosomal protein of 110 kDa,Cep1,Cep110,Cep110,Cntrl,Mouse,Mus musculus
EIAAB08838 Centrosomal protein 4,Centrosomal protein of 135 kDa,Cep135,CEP135,CEP4,Homo sapiens,Human,KIAA0635
EIAAB08839 Centrosomal protein 4,Centrosomal protein of 135 kDa,Cep135,Cep135,Cep4,Kiaa0635,Mouse,Mus musculus
EIAAB09250 68 kDa chondrocyte-expressed protein,ASPIC,ASPIC1,Cartilage acidic protein 1,CEP68,CEP-68,CRTAC1,Homo sapiens,Human
EIAAB09249 68 kDa chondrocyte-expressed protein,ASPIC,Aspic1,Cartilage acidic protein 1,Cep68,CEP-68,Crtac1,Mouse,Mus musculus,Protein CRTAC1-B


 

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