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

ISWI chromatin-remodeling complex ATPase ISW2 (EC 3.6.4.-) (Imitation switch protein 2)

 ISW2_YEAST              Reviewed;        1120 AA.
Q08773; D6W303;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-APR-2018, entry version 157.
RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2;
EC=3.6.4.-;
AltName: Full=Imitation switch protein 2;
Name=ISW2; OrderedLocusNames=YOR304W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[2]
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).
[3]
IDENTIFICATION IN THE ISW2 COMPLEX, FUNCTION, AND MUTAGENESIS OF
LYS-215.
PubMed=10090725; DOI=10.1101/gad.13.6.686;
Tsukiyama T., Palmer J., Landel C.C., Shiloach J., Wu C.;
"Characterization of the imitation switch subfamily of ATP-dependent
chromatin-remodeling factors in Saccharomyces cerevisiae.";
Genes Dev. 13:686-697(1999).
[4]
FUNCTION OF THE ISW2 COMPLEX.
PubMed=11081629; DOI=10.1016/S0092-8674(00)00134-3;
Goldmark J.P., Fazzio T.G., Estep P.W., Church G.M., Tsukiyama T.;
"The Isw2 chromatin remodeling complex represses early meiotic genes
upon recruitment by Ume6p.";
Cell 103:423-433(2000).
[5]
FUNCTION.
PubMed=11238381; DOI=10.1101/gad.190301;
Kent N.A., Karabetsou N., Politis P.K., Mellor J.;
"In vivo chromatin remodeling by yeast ISWI homologs Isw1p and
Isw2p.";
Genes Dev. 15:619-626(2001).
[6]
FUNCTION OF THE ISW2 COMPLEX.
PubMed=11489850; DOI=10.1128/JB.183.17.4985-4993.2001;
Sugiyama M., Nikawa J.;
"The Saccharomyces cerevisiae Isw2p-Itc1p complex represses INO1
expression and maintains cell morphology.";
J. Bacteriol. 183:4985-4993(2001).
[7]
FUNCTION OF THE ISW2 COMPLEX, AND INTERACTION WITH ITC1.
PubMed=11238944; DOI=10.1128/MCB.21.6.2098-2106.2001;
Gelbart M.E., Rechsteiner T., Richmond T.J., Tsukiyama T.;
"Interactions of Isw2 chromatin remodeling complex with nucleosomal
arrays: analyses using recombinant yeast histones and immobilized
templates.";
Mol. Cell. Biol. 21:2098-2106(2001).
[8]
FUNCTION OF THE ISW2 COMPLEX.
PubMed=11533234; DOI=10.1128/MCB.21.19.6450-6460.2001;
Fazzio T.G., Kooperberg C., Goldmark J.P., Neal C., Basom R.,
Delrow J., Tsukiyama T.;
"Widespread collaboration of Isw2 and Sin3-Rpd3 chromatin remodeling
complexes in transcriptional repression.";
Mol. Cell. Biol. 21:6450-6460(2001).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
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).
[11]
IDENTIFICATION IN THE ISW2 COMPLEX, AND FUNCTION OF THE ISW2 COMPLEX.
PubMed=14673157; DOI=10.1128/MCB.24.1.217-227.2004;
Iida T., Araki H.;
"Noncompetitive counteractions of DNA polymerase epsilon and
ISW2/yCHRAC for epigenetic inheritance of telomere position effect in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 24:217-227(2004).
[12]
IDENTIFICATION IN THE ISW2 COMPLEX.
PubMed=15024052; DOI=10.1128/MCB.24.7.2605-2613.2004;
McConnell A.D., Gelbart M.E., Tsukiyama T.;
"Histone fold protein Dls1p is required for Isw2-dependent chromatin
remodeling in vivo.";
Mol. Cell. Biol. 24:2605-2613(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; THR-1079 AND
SER-1082, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-19; SER-831;
THR-1079 AND SER-1082, 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).
-!- FUNCTION: Catalytic component of the ISW2 complex, which acts in
remodeling the chromatin by catalyzing an ATP-dependent alteration
in the structure of nucleosomal DNA. The ISW2 complex is involved
in coordinating transcriptional repression and in inheritance of
telomeric silencing. It is involved in repression of MAT a-
specific genes, INO1, and early meiotic genes during mitotic
growth dependent upon transcription factor UME6 and in a parallel
pathway to the RPD3-SIN3 histone deacetylase complex.
{ECO:0000269|PubMed:10090725, ECO:0000269|PubMed:11081629,
ECO:0000269|PubMed:11238381, ECO:0000269|PubMed:11238944,
ECO:0000269|PubMed:11489850, ECO:0000269|PubMed:11533234,
ECO:0000269|PubMed:14673157}.
-!- SUBUNIT: Component of the ISW2 complex, which at least consists of
ISW2, ITC1, DLS1 and DPB4. May form a stable subcomplex with ITC1.
{ECO:0000269|PubMed:10090725, ECO:0000269|PubMed:14673157,
ECO:0000269|PubMed:15024052}.
-!- INTERACTION:
P40366:DLS1; NbExp=9; IntAct=EBI-31118, EBI-25910;
P38144:ISW1; NbExp=3; IntAct=EBI-31118, EBI-21087;
P53125:ITC1; NbExp=4; IntAct=EBI-31118, EBI-23967;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00624, ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z75212; CAA99622.1; -; Genomic_DNA.
EMBL; BK006948; DAA11069.1; -; Genomic_DNA.
PIR; S67208; S67208.
RefSeq; NP_014948.1; NM_001183724.1.
ProteinModelPortal; Q08773; -.
SMR; Q08773; -.
BioGrid; 34692; 336.
DIP; DIP-6603N; -.
IntAct; Q08773; 55.
MINT; Q08773; -.
STRING; 4932.YOR304W; -.
iPTMnet; Q08773; -.
MaxQB; Q08773; -.
PaxDb; Q08773; -.
PRIDE; Q08773; -.
EnsemblFungi; YOR304W; YOR304W; YOR304W.
GeneID; 854480; -.
KEGG; sce:YOR304W; -.
EuPathDB; FungiDB:YOR304W; -.
SGD; S000005831; ISW2.
GeneTree; ENSGT00900000140963; -.
HOGENOM; HOG000192862; -.
InParanoid; Q08773; -.
KO; K11654; -.
OMA; MAFTEWI; -.
OrthoDB; EOG092C1YH4; -.
BioCyc; YEAST:G3O-33788-MONOMER; -.
PRO; PR:Q08773; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0008623; C:CHRAC; IPI:SGD.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0005634; C:nucleus; IPI:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019237; F:centromeric DNA binding; IDA:SGD.
GO; GO:0003682; F:chromatin binding; IDA:SGD.
GO; GO:0015616; F:DNA translocase activity; IDA:SGD.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IEA:InterPro.
GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
GO; GO:0000183; P:chromatin silencing at rDNA; IMP:SGD.
GO; GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
GO; GO:0060195; P:negative regulation of antisense RNA transcription; IGI:SGD.
GO; GO:0046020; P:negative regulation of transcription from RNA polymerase II promoter by pheromones; IMP:SGD.
GO; GO:0016584; P:nucleosome positioning; IDA:SGD.
GO; GO:0006369; P:termination of RNA polymerase II transcription; IGI:SGD.
CDD; cd00079; HELICc; 1.
CDD; cd00167; SANT; 1.
Gene3D; 1.10.1040.30; -; 1.
Gene3D; 3.40.50.10810; -; 1.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR015194; ISWI_HAND-dom.
InterPro; IPR036306; ISWI_HAND-dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
InterPro; IPR015195; SLIDE.
InterPro; IPR038718; SNF2-like_sf.
InterPro; IPR000330; SNF2_N.
Pfam; PF09110; HAND; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF09111; SLIDE; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00717; SANT; 2.
SUPFAM; SSF101224; SSF101224; 2.
SUPFAM; SSF46689; SSF46689; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51293; SANT; 1.
1: Evidence at protein level;
ATP-binding; Chromatin regulator; Complete proteome; DNA-binding;
Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 1120 ISWI chromatin-remodeling complex ATPase
ISW2.
/FTId=PRO_0000240453.
DOMAIN 196 361 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 494 645 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 886 938 SANT. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
NP_BIND 209 216 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 312 315 DEAH box.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 831 831 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 1079 1079 Phosphothreonine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 1082 1082 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MUTAGEN 215 215 K->A: Abolishes ATPase activity.
{ECO:0000269|PubMed:10090725}.
SEQUENCE 1120 AA; 130327 MW; F71007D7B25C9348 CRC64;
MTTQQEEQRS DTKNSKSESP SEVLVDTLDS KSNGSSDDDN IGQSEELSDK EIYTVEDRPP
EYWAQRKKKF VLDVDPKYAK QKDKSDTYKR FKYLLGVTDL FRHFIGIKAK HDKNIQKLLK
QLDSDANKLS KSHSTVSSSS RHHRKTEKEE DAELMADEEE EIVDTYQEDI FVSESPSFVK
SGKLRDYQVQ GLNWLISLHE NKLSGILADE MGLGKTLQTI SFLGYLRYVK QIEGPFLIIV
PKSTLDNWRR EFLKWTPNVN VLVLHGDKDT RADIVRNIIL EARFDVLITS YEMVIREKNA
LKRLAWQYIV IDEAHRIKNE QSALSQIIRL FYSKNRLLIT GTPLQNNLHE LWALLNFLLP
DIFGDSELFD EWFEQNNSEQ DQEIVIQQLH SVLNPFLLRR VKADVEKSLL PKIETNVYVG
MTDMQIQWYK SLLEKDIDAV NGAVGKREGK TRLLNIVMQL RKCCNHPYLF EGAEPGPPYT
TDEHLIFNSG KMIILDKLLK RLKEKGSRVL IFSQMSRLLD ILEDYCYFRD FEYCRIDGST
SHEERIEAID EYNKPNSEKF VFLLTTRAGG LGINLVTADT VILFDSDWNP QADLQAMDRA
HRIGQKKQVH VYRFVTENAI EEKVIERAAQ KLRLDQLVIQ QGTGKKTASL GNSKDDLLDM
IQFGAKNMFE KKASKVTVDA DIDDILKKGE QKTQELNAKY QSLGLDDLQK FNGIENQSAY
EWNGKSFQKK SNDKVVEWIN PSRRERRREQ TTYSVDDYYK EIIGGGSKSA SKQTPQPKAP
RAPKVIHGQD FQFFPKELDA LQEKEQLYFK KKVNYKVTSY DITGDIRNEG SDAEEEEGEY
KNAANTEGHK GHEELKRRIE EEQEKINSAP DFTQEDELRK QELISKAFTN WNKRDFMAFI
NACAKYGRDD MENIKKSIDS KTPEEVEVYA KIFWERLKEI NGWEKYLHNV ELGEKKNEKL
KFQETLLRQK IEQCKHPLHE LIIQYPPNNA RRTYNTLEDK FLLLAVNKYG LRADKLYEKL
KQEIMMSDLF TFDWFIKTRT VHELSKRVHT LLTLIVREYE QPDANKKKRS RTSATREDTP
LSQNESTRAS TVPNLPTTMV TNQKDTNDHV DKRTKIDQEA


Related products :

Catalog number Product name Quantity
EIAAB36191 HBV pX-associated protein 8,HBXAP,Hepatitis B virus X-associated protein,Homo sapiens,Human,p325 subunit of RSF chromatin-remodeling complex,Remodeling and spacing factor 1,RSF1,Rsf-1,XAP8
28-823 SMARCE1 is part of the large ATP-dependent chromatin remodeling complex SWI_SNF, which is required for transcriptional activation of genes normally repressed by chromatin. The protein, either alone or 0.05 mg
31-193 Brg- or hBrm-associated factor (BAF) complexes, a chromatin-remodeling complex family of mammalian cells, facilitate transcriptional activity by remodeling nucleosome structure. Brg1 is the core subun 0.1 mg
27-242 Brg- or hBrm-associated factor (BAF) complexes, a chromatin-remodeling complex family of mammalian cells, facilitate transcriptional activity by remodeling nucleosome structure. Brg1 is the core subun 0.05 mg
27-258 Brg- or hBrm-associated factor (BAF) complexes, a chromatin-remodeling complex family of mammalian cells, facilitate transcriptional activity by remodeling nucleosome structure. Brg1 is the core subun 0.05 mg
25-194 DPF3 is a muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleoso 0.05 mg
EIAAB07147 AD-013,ATP-dependent helicase CHD9,CHD9,CHD-9,Chromatin-related mesenchymal modulator,Chromatin-remodeling factor CHROM1,Chromodomain-helicase-DNA-binding protein 9,CReMM,Homo sapiens,Human,KIAA0308,K
EIAAB07249 CHRAC1,CHRAC-1,CHRAC15,CHRAC-15,Chromatin accessibility complex 15 kDa protein,Chromatin accessibility complex protein 1,DNA polymerase epsilon subunit p15,Homo sapiens,HuCHRAC15,Human
EIAAB33908 CAF-1 subunit C,CAF-I 48 kDa subunit,CAF-I p48,Chromatin assembly factor 1 subunit C,Chromatin assembly factor I p48 subunit,Histone-binding protein RBBP4,Homo sapiens,Human,Nucleosome-remodeling fact
EIAAB33905 CAF-1 subunit C,CAF-I 48 kDa subunit,CAF-I p48,Chromatin assembly factor 1 subunit C,Chromatin assembly factor I p48 subunit,Histone-binding protein RBBP4,Mouse,Mus musculus,Nucleosome-remodeling fact
29-130 MSL3L1 is a nuclear protein, which is thought to play a similar function in chromatin remodeling and transcriptional regulation. This gene has been found to undergo X inactivation. 0.1 mg
26-348 RSF1 (HBXAP) is involved in transcription repression, transcription coactivation when associated with hepatitis B virus X protein (HBX), and chromatin remodeling and spacing when associated with SNF2H 0.05 mg
30-704 MSL3L2 contains 1 chromo domain. It may be involved in chromatin remodeling and transcriptional regulation. 0.05 mg
26-579 MSL3L2 contains 1 chromo domain. It may be involved in chromatin remodeling and transcriptional regulation. 0.05 mg
EIAAB40078 Chromatin-specific transcription elongation factor 80 kDa subunit,Facilitates chromatin transcription complex 80 kDa subunit,Facilitates chromatin transcription complex subunit SSRP1,FACT 80 kDa subun
25-553 MSL3L1 is a nuclear protein, which is thought to play a similar function in chromatin remodeling and transcriptional regulation. This gene has been found to undergo X inactivation. This gene encodes a 0.05 mg
28-944 HTATIP belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein. HATs play important roles in regulating chromatin remodeling, t 0.05 mg
26-111 NCAPH is a member of the barr family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. The protein is a 0.05 mg
30-178 NCAPH is a member of the barr family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. The protein is a 0.05 mg
25-498 PBRM1 is involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). 0.05 mg
30-174 NCAPD2 is the regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces p 0.05 mg
EIAAB07248 Chrac1,CHRAC-1,Chromatin accessibility complex protein 1,DNA polymerase epsilon subunit p15,Mouse,Mus musculus,NF-YC-like protein,YCL1,YC-like protein 1
CHRC1_HUMAN Human ELISA Kit FOR Chromatin accessibility complex protein 1 96T
CSB-EL005376HU Human Chromatin accessibility complex protein 1(CHRAC1) ELISA kit 96T
CSB-EL005376MO Mouse Chromatin accessibility complex protein 1(CHRAC1) ELISA kit 96T


 

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