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

Resistance to glucose repression protein 1 (Protein HEX2) (Second-site suppressor of the rna1-1 mutation 1)

 REG1_YEAST              Reviewed;        1014 AA.
Q00816; D6VS13;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
12-SEP-2018, entry version 168.
RecName: Full=Resistance to glucose repression protein 1;
AltName: Full=Protein HEX2;
AltName: Full=Second-site suppressor of the rna1-1 mutation 1;
Name=REG1; Synonyms=HEX2, PZF240, SPP43, SRN1;
OrderedLocusNames=YDR028C; ORFNames=YD9813.06C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1889400; DOI=10.1111/j.1432-1033.1991.tb16187.x;
Niederacher D., Entian K.-D.;
"Characterization of Hex2 protein, a negative regulatory element
necessary for glucose repression in yeast.";
Eur. J. Biochem. 200:311-319(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1588964; DOI=10.1128/MCB.12.6.2673;
Tung K.-S., Norbeck L.L., Nolan S.L., Atkinson N.S., Hopper A.K.;
"SRN1, a yeast gene involved in RNA processing, is identical to
HEX2/REG1, a negative regulator in glucose repression.";
Mol. Cell. Biol. 12:2673-2680(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1014.
PubMed=8896275;
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1085::AID-YEA9>3.3.CO;2-S;
Eide L.G., Sander C., Prydz H.;
"Sequencing and analysis of a 35.4 kb region on the right arm of
chromosome IV from Saccharomyces cerevisiae reveal 23 open reading
frames.";
Yeast 12:1085-1090(1996).
[6]
INTERACTION WITH PP1.
PubMed=8846786;
Tu J.L., Carlson M.;
"REG1 binds to protein phosphatase type 1 and regulates glucose
repression in Saccharomyces cerevisiae.";
EMBO J. 14:5939-5946(1995).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-75, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-421; SER-572 AND
SER-576, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-73; SER-75; TYR-480 AND
SER-490, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-254; SER-311;
SER-421; SER-576 AND SER-680, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-242; SER-421;
SER-570; SER-572; SER-576; SER-610; SER-614; THR-896; SER-898 AND
SER-980, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[13]
FUNCTION, AND INTERACTION WITH SAK1.
PubMed=21216941; DOI=10.1128/EC.00291-10;
Liu Y., Xu X., Carlson M.;
"Interaction of SNF1 protein kinase with its activating kinase Sak1.";
Eukaryot. Cell 10:313-319(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Involved in RNA processing and negative regulation of
glucose repression. Regulates the level of two antigens, P43 and
P70. Binds to protein phosphatase type 1. Functions with REG2 and
SNF1 protein kinase to regulate growth. Might regulate SNF1
directly or indirectly. {ECO:0000269|PubMed:21216941}.
-!- SUBUNIT: Interacts with SAK1. {ECO:0000269|PubMed:21216941,
ECO:0000269|PubMed:8846786}.
-!- INTERACTION:
P32598:GLC7; NbExp=4; IntAct=EBI-8270, EBI-13715;
P06782:SNF1; NbExp=7; IntAct=EBI-8270, EBI-17516;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 2560 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M33703; AAA34670.1; -; Genomic_DNA.
EMBL; M90540; AAB59326.1; -; Genomic_DNA.
EMBL; Z47814; CAA87807.1; -; Genomic_DNA.
EMBL; Z74324; CAA98850.1; -; Genomic_DNA.
EMBL; X95966; CAA65223.1; -; Genomic_DNA.
EMBL; BK006938; DAA11873.1; -; Genomic_DNA.
PIR; S32613; S32613.
RefSeq; NP_010311.1; NM_001180336.1.
ProteinModelPortal; Q00816; -.
SMR; Q00816; -.
BioGrid; 32078; 137.
ComplexPortal; CPX-1266; REG1-GLC7 phosphatase complex.
DIP; DIP-2513N; -.
ELM; Q00816; -.
IntAct; Q00816; 24.
MINT; Q00816; -.
STRING; 4932.YDR028C; -.
iPTMnet; Q00816; -.
MaxQB; Q00816; -.
PaxDb; Q00816; -.
PRIDE; Q00816; -.
EnsemblFungi; YDR028C; YDR028C; YDR028C.
GeneID; 851592; -.
KEGG; sce:YDR028C; -.
EuPathDB; FungiDB:YDR028C; -.
SGD; S000002435; REG1.
InParanoid; Q00816; -.
OMA; TRSMGLL; -.
OrthoDB; EOG092C22EU; -.
BioCyc; YEAST:G3O-29644-MONOMER; -.
PRO; PR:Q00816; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000164; C:protein phosphatase type 1 complex; TAS:SGD.
GO; GO:0005773; C:vacuole; IEA:GOC.
GO; GO:0019888; F:protein phosphatase regulator activity; TAS:SGD.
GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
GO; GO:0005977; P:glycogen metabolic process; TAS:SGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:SGD.
GO; GO:0007039; P:protein catabolic process in the vacuole; IDA:SGD.
GO; GO:0006109; P:regulation of carbohydrate metabolic process; IGI:SGD.
GO; GO:0006986; P:response to unfolded protein; IMP:SGD.
GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
InterPro; IPR013860; AreA_GATA.
Pfam; PF08550; DUF1752; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:22814378}.
CHAIN 2 1014 Resistance to glucose repression protein
1.
/FTId=PRO_0000083953.
MOTIF 277 283 Nuclear localization signal.
{ECO:0000255}.
MOTIF 595 599 Nuclear localization signal.
{ECO:0000255}.
MOTIF 873 879 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 543 552 Ser-rich.
COMPBIAS 742 760 Asp/Glu-rich (acidic).
COMPBIAS 834 844 Asp/Glu-rich (acidic).
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:22814378}.
MOD_RES 73 73 Phosphothreonine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 254 254 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 480 480 Phosphotyrosine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 576 576 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 614 614 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 896 896 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 898 898 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 980 980 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
CONFLICT 376 377 DK -> EE (in Ref. 1; AAA34670).
{ECO:0000305}.
CONFLICT 534 534 N -> K (in Ref. 1; AAA34670).
{ECO:0000305}.
CONFLICT 657 657 D -> H (in Ref. 1; AAA34670).
{ECO:0000305}.
CONFLICT 889 889 S -> T (in Ref. 1; AAA34670).
{ECO:0000305}.
CONFLICT 988 1014 ARGMASKYLHSWKKSDVKPQENGNDSS -> QEVWQASTCT
LGKRVTSSHKKMEMTAVRRKNFEVNMKRK (in Ref.
1). {ECO:0000305}.
SEQUENCE 1014 AA; 112616 MW; 0D4AAC75E111B346 CRC64;
MSTNLANYFA GKKDIENEHV NRNASHESNS KSDVKISGND NDNDEDMGPS VSMAVQAKND
DDFHKSTFNL KRTRSMGLLD EYIDPTKKLL GRSDDLYDND NEYYDNSSNN SSSNSSDDDY
DDGYQEHSTS VSPPPADNDS YLIPQDDNDV VVEPERHVDY LSHEWKESEI SNSWKYIILK
KKKRDVDLVN AARLENASWR TWAKARNNLK TVSPEVVNWS KDSDVTWLYG PIVRDSEGNA
QSEEEHDLER GYGSDDENSK RISMPTKNSK SIAAAPKPIL KKRTVTEIIE DNALWKLNEA
RKHMTEMKHA SVIMDPNGNK NVHDDFDALA AQVNAQYYHY PKESNSSVSL KSQHSDKKDN
STIPNPVGEN SNGGGDKGEE DLHLKSALHV QNNRSTAQSN KSILENSTND RKANLDQNLN
SPDNNRFPSS TSSSNRDNEN NSMGLSSILT SNPSEKSNKP TKNRHIHFND RVEQCMALRY
PASQSEDDES DDENKQYVDV NNNANVTTIN NNRTPLLAIQ HKSIPINSAT EHLNKNTSDD
DTSSQSSSSS HSDDEEHGGL YINARFSRRS DSGVHSPITD NSSVASSTTS RAHVRPIIKL
LPDTTLNYGS DEESDNGEFN GYGNAVSHNV NTSRGYDYIY DYNSVYTGDT SSFLPVDSCD
IVDVPEGMDL QTAIADDNAS NYEFNNAVES KEKHVPQLHK ASANNTTRQH GSHMLLYDDD
NYSSSSDSEQ QFIEDSQYNS SDDEEEEDDD DQEVDDNHDE GLSLRRTLSL GKSGSTNSLY
DLAQPSLSSA TPQQKNPTNF TGGKTDVDKD AQLAVRPYPL KRNSSSGNFI FNSDSEEESS
SEEEQRPLPA NSQLVNRSVL KGSVTPANIS SQKKKALPKQ PKASDSSQSF RIVNNTPSPA
EVGASDVAIE GYFSPRNESI KSVVSGGNMM DHQDHSEMDT LAKGFENCHI NNASKLKDKK
VDSVQTTRKE ASLTDSSNES LHKVVQNARG MASKYLHSWK KSDVKPQENG NDSS


Related products :

Catalog number Product name Quantity
EIAAB25874 Influenza resistance protein,Interferon-induced GTP-binding protein Mx1,Mouse,Mus musculus,Mx1,Myxoma resistance protein 1,Myxovirus resistance protein 1
EIAAB04804 AKI1,Akt kinase-interacting protein 1,CC2D1A,Coiled-coil and C2 domain-containing protein 1A,Five repressor element under dual repression-binding protein 1,FRE under dual repression-binding protein 1,
EIAAB04805 Cc2d1a,Coiled-coil and C2 domain-containing protein 1A,Five repressor element under dual repression-binding protein 1,FRE under dual repression-binding protein 1,Freud-1,Rat,Rattus norvegicus
EIAAB04803 Cc2d1a,Coiled-coil and C2 domain-containing protein 1A,Five repressor element under dual repression-binding protein 1,FRE under dual repression-binding protein 1,Freud-1,Mouse,Mus musculus
25-495 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.05 mg
27-738 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.1 mg
29-041 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.05 mg
27-739 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.05 mg
orb80846 Human Phosphoinositide 3-kinase p110g inactive mutant protein The PI3KdD946A protein is catalytically inactive mutant of PI3Kd with D946A mutation in the ATP binding site. This recombinant catalytical 1
20-783-74648 MOUSE ANTI HUMAN BREAST CANCER RESISTANCE PROTEIN - Placenta-specific ATP-binding cassette transporter; Breast cancer resistance protein; Mitoxantrone resistance-associated protein; CD338 antigen; CDw 1 ml
EIAAB25335 Mannose-P-dolichol utilization defect 1 protein,Mouse,Mpdu1,Mus musculus,SL15,Supl15h,Suppressor of Lec15 and Lec35 glycosylation mutation homolog
EIAAB25336 Homo sapiens,Human,Mannose-P-dolichol utilization defect 1 protein,MPDU1,SL15,Suppressor of Lec15 and Lec35 glycosylation mutation homolog
25-743 RIOK3 was identified by the similarity to the Aspergillus nidulans SUDD protein, an extragenic suppressor of the heat-sensitive bimD6 mutation that fails to attach properly to the spindle microtubules 0.05 mg
EIAAB25876 Interferon-induced GTP-binding protein Mx1,Mx1,Myxoma resistance protein 1,Myxovirus resistance protein 1,Rat,Rattus norvegicus
EIAAB25877 Bos taurus,Bovine,Interferon-induced GTP-binding protein Mx1,MX1,Myxoma resistance protein 1,Myxovirus resistance protein 1
EIAAB25875 Interferon-induced GTP-binding protein Mx1,MX1,Myxoma resistance protein 1,Myxovirus resistance protein 1,Pig,Sus scrofa
30-622 ING1 is a tumor suppressor protein that can induce cell growth arrest and apoptosis. The protein is a nuclear protein that physically interacts with the tumor suppressor protein TP53 and is a componen 0.1 mg
EIAAB07483 Centrosomal protein C10orf90 homolog,D7Ertd443e,Fats,Fragile-site associated tumor suppressor,Mouse,Mus musculus
EIAAB25880 Homo sapiens,Human,Interferon-induced GTP-binding protein Mx2,Interferon-regulated resistance GTP-binding protein MxB,MX2,Myxovirus resistance protein 2,p78-related protein
25-070 SIN3A is a transcriptional regulatory protein. It contains paired amphipathic helix (PAH) domains, which are important for protein-protein interactions and may mediate repression by the Mad-Max comple 0.05 mg
EIAAB25437 ABCC6,Anthracycline resistance-associated protein,ARA,ATP-binding cassette sub-family C member 6,Homo sapiens,Human,MOAT-E,MRP6,Multidrug resistance-associated protein 6,Multi-specific organic anion t
U0960h CLIA ABCG2,ABCP,ATP-binding cassette sub-family G member 2,BCRP,BCRP1,Breast cancer resistance protein,CDw338,Homo sapiens,Human,Mitoxantrone resistance-associated protein,MXR,Placenta-specific ATP-bi 96T
E0960h ELISA ABCG2,ABCP,ATP-binding cassette sub-family G member 2,BCRP,BCRP1,Breast cancer resistance protein,CDw338,Homo sapiens,Human,Mitoxantrone resistance-associated protein,MXR,Placenta-specific ATP-b 96T
E0960h ELISA kit ABCG2,ABCP,ATP-binding cassette sub-family G member 2,BCRP,BCRP1,Breast cancer resistance protein,CDw338,Homo sapiens,Human,Mitoxantrone resistance-associated protein,MXR,Placenta-specific 96T
EIAAB25873 Canis familiaris,Canis lupus familiaris,Dog,Interferon-induced GTP-binding protein Mx1,MX1,Myxoma resistance protein 1,Myxovirus resistance protein 1


 

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