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

GATOR complex protein WDR24 (WD repeat-containing protein 24)

 WDR24_HUMAN             Reviewed;         920 AA.
Q96S15; A2IDB8; D3DU59; Q96GC7; Q9H0B7;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
05-DEC-2018, entry version 149.
RecName: Full=GATOR complex protein WDR24 {ECO:0000305};
AltName: Full=WD repeat-containing protein 24 {ECO:0000312|HGNC:HGNC:20852};
Name=WDR24 {ECO:0000312|HGNC:HGNC:20852};
Synonyms=C16orf21 {ECO:0000312|HGNC:HGNC:20852};
ORFNames=JFP7 {ECO:0000312|EMBL:AAK61244.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=11157797; DOI=10.1093/hmg/10.4.339;
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
Higgs D.R.;
"Sequence, structure and pathology of the fully annotated terminal 2
Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney, and Lung;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-626 AND
THR-711, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[8]
INTERACTION WITH SESN1; SESN2 AND SESN3.
PubMed=25263562; DOI=10.1016/j.celrep.2014.09.014;
Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M.,
Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.;
"The Sestrins interact with GATOR2 to negatively regulate the amino-
acid-sensing pathway upstream of mTORC1.";
Cell Rep. 9:1-8(2014).
[9]
INTERACTION WITH SESN2.
PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019;
Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C.,
Akopiants K., Guan K.L., Karin M., Budanov A.V.;
"Sestrins inhibit mTORC1 kinase activation through the GATOR
complex.";
Cell Rep. 9:1281-1291(2014).
[10]
FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND SUBUNIT.
PubMed=23723238; DOI=10.1126/science.1232044;
Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W.,
Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M.,
Sabatini D.M.;
"A Tumor suppressor complex with GAP activity for the Rag GTPases that
signal amino acid sufficiency to mTORC1.";
Science 340:1100-1106(2013).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 AND SER-626, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
INTERACTION WITH CASTOR2 AND CASTOR1.
PubMed=26972053; DOI=10.1016/j.cell.2016.02.035;
Chantranupong L., Scaria S.M., Saxton R.A., Gygi M.P., Shen K.,
Wyant G.A., Wang T., Harper J.W., Gygi S.P., Sabatini D.M.;
"The CASTOR proteins are arginine sensors for the mTORC1 pathway.";
Cell 165:153-164(2016).
[13]
FUNCTION.
PubMed=27487210; DOI=10.1038/nature19079;
Saxton R.A., Chantranupong L., Knockenhauer K.E., Schwartz T.U.,
Sabatini D.M.;
"Mechanism of arginine sensing by CASTOR1 upstream of mTORC1.";
Nature 536:229-233(2016).
[14]
FUNCTION, AND INTERACTION WITH SESN2.
PubMed=26449471; DOI=10.1126/science.aab2674;
Wolfson R.L., Chantranupong L., Saxton R.A., Shen K., Scaria S.M.,
Cantor J.R., Sabatini D.M.;
"Sestrin2 is a leucine sensor for the mTORC1 pathway.";
Science 351:43-48(2016).
[15]
FUNCTION, AND INTERACTION WITH SESN2.
PubMed=26586190; DOI=10.1126/science.aad2087;
Saxton R.A., Knockenhauer K.E., Wolfson R.L., Chantranupong L.,
Pacold M.E., Wang T., Schwartz T.U., Sabatini D.M.;
"Structural basis for leucine sensing by the Sestrin2-mTORC1
pathway.";
Science 351:53-58(2016).
[16]
FUNCTION.
PubMed=27166823; DOI=10.1371/journal.pgen.1006036;
Cai W., Wei Y., Jarnik M., Reich J., Lilly M.A.;
"The GATOR2 component Wdr24 regulates TORC1 activity and lysosome
function.";
PLoS Genet. 12:E1006036-E1006036(2016).
[17]
SUBCELLULAR LOCATION.
PubMed=28199306; DOI=10.1038/nature21423;
Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M.,
Shen K., Condon K.J., Petri S., Kedir J., Scaria S.M.,
Abu-Remaileh M., Frankel W.N., Sabatini D.M.;
"KICSTOR recruits GATOR1 to the lysosome and is necessary for
nutrients to regulate mTORC1.";
Nature 543:438-442(2017).
-!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
within the amino acid-sensing branch of the TORC1 signaling
pathway (PubMed:23723238, PubMed:27166823). Indirectly activates
mTORC1 and the TORC1 signaling pathway through the inhibition of
the GATOR1 subcomplex (PubMed:23723238). It is negatively
regulated by the upstream amino acid sensors SESN2 and CASTOR1
(PubMed:26449471, PubMed:26586190, PubMed:27487210). In addition
to its role in regulation of the TORC1 complex, promotes the
acidification of lysosomes and facilitates autophagic flux
(PubMed:27166823). {ECO:0000269|PubMed:23723238,
ECO:0000269|PubMed:26449471, ECO:0000269|PubMed:26586190,
ECO:0000269|PubMed:27166823, ECO:0000269|PubMed:27487210}.
-!- SUBUNIT: Within the GATOR complex, component of the GATOR2
subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR
complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC
heterodimers (PubMed:23723238). The GATOR2 complex interacts with
CASTOR2 and CASTOR1; the interaction is negatively regulated by
arginine (PubMed:26972053). The GATOR2 complex interacts with
SESN1, SESN2 and SESN3; the interaction is negatively regulated by
amino acids (PubMed:25263562, PubMed:25457612, PubMed:26449471,
PubMed:26586190). {ECO:0000269|PubMed:23723238,
ECO:0000269|PubMed:25263562, ECO:0000269|PubMed:25457612,
ECO:0000269|PubMed:26449471, ECO:0000269|PubMed:26586190,
ECO:0000269|PubMed:26972053}.
-!- INTERACTION:
Q92624:APPBP2; NbExp=4; IntAct=EBI-746424, EBI-743771;
Q9NXC5:MIOS; NbExp=15; IntAct=EBI-746424, EBI-2515122;
P58004:SESN2; NbExp=17; IntAct=EBI-746424, EBI-3939642;
P58005:SESN3; NbExp=3; IntAct=EBI-746424, EBI-16179942;
Q5T011:SZT2; NbExp=5; IntAct=EBI-746424, EBI-10749411;
Q6PJI9:WDR59; NbExp=8; IntAct=EBI-746424, EBI-2515073;
-!- SUBCELLULAR LOCATION: Lysosome membrane
{ECO:0000269|PubMed:28199306}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96S15-1; Sequence=Displayed;
Name=2;
IsoId=Q96S15-2; Sequence=VSP_016180, VSP_016181;
-!- SIMILARITY: Belongs to the WD repeat WDR24 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AE006464; AAK61244.1; -; Genomic_DNA.
EMBL; AL136863; CAB66797.1; -; mRNA.
EMBL; Z92544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85752.1; -; Genomic_DNA.
EMBL; CH471112; EAW85753.1; -; Genomic_DNA.
EMBL; BC008025; AAH08025.1; -; mRNA.
EMBL; BC009761; AAH09761.2; -; mRNA.
CCDS; CCDS10420.1; -. [Q96S15-2]
RefSeq; NP_115635.1; NM_032259.3. [Q96S15-2]
UniGene; Hs.459632; -.
ProteinModelPortal; Q96S15; -.
BioGrid; 123953; 24.
CORUM; Q96S15; -.
DIP; DIP-53812N; -.
IntAct; Q96S15; 19.
STRING; 9606.ENSP00000293883; -.
iPTMnet; Q96S15; -.
PhosphoSitePlus; Q96S15; -.
DMDM; 74762692; -.
EPD; Q96S15; -.
MaxQB; Q96S15; -.
PaxDb; Q96S15; -.
PeptideAtlas; Q96S15; -.
PRIDE; Q96S15; -.
ProteomicsDB; 78052; -.
ProteomicsDB; 78053; -. [Q96S15-2]
DNASU; 84219; -.
Ensembl; ENST00000248142; ENSP00000248142; ENSG00000127580. [Q96S15-1]
Ensembl; ENST00000293883; ENSP00000293883; ENSG00000127580. [Q96S15-2]
GeneID; 84219; -.
KEGG; hsa:84219; -.
UCSC; uc002ciz.2; human. [Q96S15-1]
CTD; 84219; -.
EuPathDB; HostDB:ENSG00000127580.15; -.
GeneCards; WDR24; -.
HGNC; HGNC:20852; WDR24.
HPA; HPA039506; -.
neXtProt; NX_Q96S15; -.
OpenTargets; ENSG00000127580; -.
PharmGKB; PA134918496; -.
eggNOG; KOG0269; Eukaryota.
eggNOG; ENOG410XSJ6; LUCA.
GeneTree; ENSGT00940000159396; -.
HOGENOM; HOG000234392; -.
HOVERGEN; HBG080644; -.
InParanoid; Q96S15; -.
KO; K20408; -.
OMA; TLCQHLF; -.
OrthoDB; EOG091G0052; -.
PhylomeDB; Q96S15; -.
TreeFam; TF314190; -.
SignaLink; Q96S15; -.
SIGNOR; Q96S15; -.
GeneWiki; WDR24; -.
GenomeRNAi; 84219; -.
PRO; PR:Q96S15; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000127580; Expressed in 105 organ(s), highest expression level in right uterine tube.
CleanEx; HS_WDR24; -.
Genevisible; Q96S15; HS.
GO; GO:0061700; C:GATOR2 complex; IDA:SGD.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
InterPro; IPR037590; WDR24.
PANTHER; PTHR22850:SF131; PTHR22850:SF131; 1.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 3.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 2.
1: Evidence at protein level;
Alternative splicing; Autophagy; Complete proteome; Lysosome;
Membrane; Phosphoprotein; Reference proteome; Repeat; WD repeat.
CHAIN 1 920 GATOR complex protein WDR24.
/FTId=PRO_0000051375.
REPEAT 134 174 WD 1.
REPEAT 180 220 WD 2.
REPEAT 291 331 WD 3.
REPEAT 335 375 WD 4.
REPEAT 379 421 WD 5.
REPEAT 425 468 WD 6.
MOD_RES 600 600 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 711 711 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 724 724 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 728 728 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CFJ9}.
VAR_SEQ 1 62 Missing (in isoform 2).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_016180.
VAR_SEQ 223 290 Missing (in isoform 2).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_016181.
SEQUENCE 920 AA; 101989 MW; 3BE3989D72973714 CRC64;
MGKKRTTSGE GRERQRLPAR RFRTTSPAAL RADSVDGGSL LAPLLGLTDR AFSDCPDLAD
GAMEKMSRVT TALGGSVLTG RTMHCHLDAP ANAISVCRDA AQVVVAGRSI FKIYAIEEEQ
FVEKLNLRVG RKPSLNLSCA DVVWHQMDEN LLATAATNGV VVTWNLGRPS RNKQDQLFTE
HKRTVNKVCF HPTEAHVLLS GSQDGFMKCF DLRRKDSVST FSGEATEAGP REWAMAGCVP
ILPVLSCRIL RLHHSFAHGP MQDAESTAND ARESWGCPLY PLGLCSGPQA GQSESVRDVQ
FSIRDYFTFA STFENGNVQL WDIRRPDRCE RMFTAHNGPV FCCDWHPEDR GWLATGGRDK
MVKVWDMTTH RAKEMHCVQT IASVARVKWR PECRHHLATC SMMVDHNIYV WDVRRPFVPA
AMFEEHRDVT TGIAWRHPHD PSFLLSGSKD SSLCQHLFRD ASQPVERANP EGLCYGLFGD
LAFAAKESLV AAESGRKPYT GDRRHPIFFK RKLDPAEPFA GLASSALSVF ETEPGGGGMR
WFVDTAERYA LAGRPLAELC DHNAKVAREL GRNQVAQTWT MLRIIYCSPG LVPTANLNHS
VGKGGSCGLP LMNSFNLKDM APGLGSETRL DRSKGDARSD TVLLDSSATL ITNEDNEETE
GSDVPADYLL GDVEGEEDEL YLLDPEHAHP EDPECVLPQE AFPLRHEIVD TPPGPEHLQD
KADSPHVSGS EADVASLAPV DSSFSLLSVS HALYDSRLPP DFFGVLVRDM LHFYAEQGDV
QMAVSVLIVL GERVRKDIDE QTQEHWYTSY IDLLQRFRLW NVSNEVVKLS TSRAVSCLNQ
ASTTLHVNCS HCKRPMSSRG WVCDRCHRCA SMCAVCHHVV KGLFVWCQGC SHGGHLQHIM
KWLEGSSHCP AGCGHLCEYS


Related products :

Catalog number Product name Quantity
CSB-EL026008MO Mouse WD repeat-containing protein 24(WDR24) ELISA kit 96T
I2631 WD repeat-containing protein 24 (WDR24), Mouse, ELISA Kit 96T
CSB-EL026008CH Chicken WD repeat-containing protein 24(WDR24) ELISA kit 96T
I2629 WD repeat-containing protein 24 (WDR24), Chicken, ELISA Kit 96T
CSB-EL026008HU Human WD repeat-containing protein 24(WDR24) ELISA kit 96T
I2630 WD repeat-containing protein 24 (WDR24), Human, ELISA Kit 96T
EIAAB46154 Mouse,Mus musculus,WD repeat-containing protein 24,Wdr24
WDR24 WDR24 Gene WD repeat domain 24
CSB-EL026008MO Mouse WD repeat-containing protein 24(WDR24) ELISA kit SpeciesMouse 96T
CSB-EL026008HU Human WD repeat-containing protein 24(WDR24) ELISA kit SpeciesHuman 96T
CSB-EL026008CH Chicken WD repeat-containing protein 24(WDR24) ELISA kit SpeciesChicken 96T
EIAAB46156 C16orf21,Homo sapiens,Human,JFP7,WD repeat-containing protein 24,WDR24
EIAAB43516 Mouse,Mus musculus,Tetratricopeptide repeat protein 15,TPR repeat protein 15,Trafficking protein particle complex subunit 12,Trappc12,Ttc15
EIAAB43515 CGI-87,Homo sapiens,Human,Tetratricopeptide repeat protein 15,TPR repeat protein 15,Trafficking protein particle complex subunit 12,TRAPPC12,TTC15
EIAAB46155 Chicken,Gallus gallus,RCJMB04_1a19,WD repeat-containing protein 24,WDR24
EIAAB14615 Afh,Fbl3a,F-box and leucine-rich repeat protein 3A,F-box_LRR-repeat protein 3,F-box_LRR-repeat protein 3A,Fbxl3,Fbxl3a,Mouse,Mus musculus,Ovtm,Protein after-hours,Protein overtime
EIAAB08269 CNPY3,CTG repeat protein 4a,CTG4A,ERDA5,Expanded repeat-domain protein CAG_CTG 5,Homo sapiens,HSPC084,Human,PRAT4A,Protein associated with TLR4,Protein canopy homolog 3,TNRC5,Trinucleotide repeat-cont
18-661-15190 Baculoviral IAP repeat-containing protein 2 - Inhibitor of apoptosis protein 2; HIAP2; HIAP-2; C-IAP1; TNFR2-TRAF signaling complex protein 2; IAP homolog B Polyclonal 0.1 mg
EIAAB44425 DCRR1,E3 ubiquitin-protein ligase TTC3,Homo sapiens,Human,Protein DCRR1,RING finger protein 105,RNF105,Tetratricopeptide repeat protein 3,TPR repeat protein 3,TPR repeat protein D,TPRD,TTC3
EIAAB44454 Homo sapiens,Human,Tetratricopeptide repeat protein 7B,Tetratricopeptide repeat protein 7-like-1,TPR repeat protein 7B,TPR repeat protein 7-like-1,TTC7B,TTC7L1
EIAAB46135 Bromodomain and WD repeat-containing protein 2,BRWD2,Homo sapiens,Human,KIAA1351,WD repeat-containing protein 11,WD repeat-containing protein 15,WDR11,WDR15
201-20-6410 WDR24{WD repeat domain 24}rabbit.pAb 0.2ml
EIAAB46365 Homo sapiens,Human,WD repeat domain phosphoinositide-interacting protein 3,WD repeat-containing protein 45-like,WDR45L,WDR45-like protein,WIPI3,WIPI-3,WIPI49-like protein
EIAAB14621 FBL4,FBL5,F-box and leucine-rich repeat protein 5,F-box protein FBL4_FBL5,F-box_LRR-repeat protein 5,FBXL5,FLR1,Homo sapiens,Human,p45SKP2-like protein
EIAAB44421 Homo sapiens,Human,Protein TBPP2A,Testis development protein NYD-SP14,Tetratricopeptide repeat protein 29,TPR repeat protein 29,TTC29


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






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