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

Histone chaperone ASF1B (Anti-silencing function protein 1 homolog B) (hAsf1) (hAsf1b) (CCG1-interacting factor A-II) (CIA-II) (hCIA-II)

 ASF1B_HUMAN             Reviewed;         202 AA.
Q9NVP2; Q53G51; Q9NVZ0;
17-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 143.
RecName: Full=Histone chaperone ASF1B;
AltName: Full=Anti-silencing function protein 1 homolog B;
Short=hAsf1;
Short=hAsf1b;
AltName: Full=CCG1-interacting factor A-II;
Short=CIA-II;
Short=hCIA-II;
Name=ASF1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TLK1 AND TLK2, AND
PHOSPHORYLATION BY TLK1 AND TLK2.
PubMed=11470414; DOI=10.1016/S0960-9822(01)00298-6;
Sillje H.H.W., Nigg E.A.;
"Identification of human Asf1 chromatin assembly factors as substrates
of Tousled-like kinases.";
Curr. Biol. 11:1068-1073(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HISTONE H3.3;
HISTONE H4 AND TAF1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12842904; DOI=10.1074/jbc.M303549200;
Umehara T., Horikoshi M.;
"Transcription initiation factor IID-interactive histone chaperone
CIA-II implicated in mammalian spermatogenesis.";
J. Biol. Chem. 278:35660-35667(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis, and Uterus;
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).
[8]
FUNCTION, AND INTERACTION WITH CHAF1A; CHAF1B AND RBBP4.
PubMed=11897662; DOI=10.1093/embo-reports/kvf068;
Mello J.A., Sillje H.H.W., Roche D.M.J., Kirschner D.B., Nigg E.A.,
Almouzni G.;
"Human Asf1 and CAF-1 interact and synergize in a repair-coupled
nucleosome assembly pathway.";
EMBO Rep. 3:329-334(2002).
[9]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN
COMPLEXES WITH CHAF1A; CHAF1B; HAT1; HISTONE H3.1; HISTONE H3.3;
HISTONE H4; NASP AND RBBP4.
PubMed=14718166; DOI=10.1016/S0092-8674(03)01064-X;
Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.;
"Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways
dependent or independent of DNA synthesis.";
Cell 116:51-61(2004).
[10]
FUNCTION.
PubMed=16151251; DOI=10.1128/EC.4.9.1583-1590.2005;
Tamburini B.A., Carson J.J., Adkins M.W., Tyler J.K.;
"Functional conservation and specialization among eukaryotic anti-
silencing function 1 histone chaperones.";
Eukaryot. Cell 4:1583-1590(2005).
[11]
FUNCTION, AND INTERACTION WITH HISTONE H3.1; HISTONE H3.3 AND HISTONE
H4.
PubMed=15664198; DOI=10.1016/j.molcel.2004.12.018;
Groth A., Ray-Gallet D., Quivy J.-P., Lukas J., Bartek J.,
Almouzni G.;
"Human Asf1 regulates the flow of S phase histones during
replicational stress.";
Mol. Cell 17:301-311(2005).
[12]
INTERACTION WITH CHAF1B; HISTONE H3 AND HISTONE H4.
PubMed=16537536; DOI=10.1074/jbc.M511590200;
Sanematsu F., Takami Y., Barman H.K., Fukagawa T., Ono T.,
Shibahara K., Nakayama T.;
"Asf1 is required for viability and chromatin assembly during DNA
replication in vertebrate cells.";
J. Biol. Chem. 281:13817-13827(2006).
[13]
INTERACTION WITH CHAF1B.
PubMed=16980972; DOI=10.1038/nsmb1147;
Tang Y., Poustovoitov M.V., Zhao K., Garfinkel M., Canutescu A.,
Dunbrack R., Adams P.D., Marmorstein R.;
"Structure of a human ASF1a-HIRA complex and insights into specificity
of histone chaperone complex assembly.";
Nat. Struct. Mol. Biol. 13:921-929(2006).
[14]
PHOSPHORYLATION AT SER-198 BY TLK2.
PubMed=20016786; DOI=10.1371/journal.pone.0008328;
Pilyugin M., Demmers J., Verrijzer C.P., Karch F., Moshkin Y.M.;
"Phosphorylation-mediated control of histone chaperone ASF1 levels by
Tousled-like kinases.";
PLoS ONE 4:E8328-E8328(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
INTERACTION WITH CDAN1, IDENTIFICATION IN A COMPLEX WITH CDNA1; ASF1A;
IPO4; HISTONES H3.2 AND H4, AND MUTAGENESIS OF ASP-36 AND ASP-37.
PubMed=22407294; DOI=10.1038/emboj.2012.55;
Ask K., Jasencakova Z., Menard P., Feng Y., Almouzni G., Groth A.;
"Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1
function in S-phase histone supply.";
EMBO J. 31:2013-2023(2012).
[18]
INTERACTION WITH CREBBP.
PubMed=24616510; DOI=10.1073/pnas.1319122111;
Das C., Roy S., Namjoshi S., Malarkey C.S., Jones D.N.,
Kutateladze T.G., Churchill M.E., Tyler J.K.;
"Binding of the histone chaperone ASF1 to the CBP bromodomain promotes
histone acetylation.";
Proc. Natl. Acad. Sci. U.S.A. 111:E1072-E1081(2014).
-!- FUNCTION: Histone chaperone that facilitates histone deposition
and histone exchange and removal during nucleosome assembly and
disassembly. Cooperates with chromatin assembly factor 1 (CAF-1)
to promote replication-dependent chromatin assembly. Does not
participate in replication-independent nucleosome deposition which
is mediated by ASF1A and HIRA. Required for spermatogenesis.
{ECO:0000269|PubMed:11897662, ECO:0000269|PubMed:12842904,
ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15664198,
ECO:0000269|PubMed:16151251}.
-!- SUBUNIT: Interacts with histone H3 (including both histone H3.1
and H3.3) and histone H4. Interacts with the CHAF1A, CHAF1B and
RBBP4 subunits of the CAF-1 complex. Interacts with HAT1, NASP,
TAF1, TLK1 and TLK2. Interacts with CDAN1. Found in a cytosolic
complex with CDAN1, ASF1A, IPO4 and histones H3.1 and H4.
Interacts with CREBBP. {ECO:0000269|PubMed:11470414,
ECO:0000269|PubMed:11897662, ECO:0000269|PubMed:12842904,
ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15664198,
ECO:0000269|PubMed:16537536, ECO:0000269|PubMed:16980972,
ECO:0000269|PubMed:22407294, ECO:0000269|PubMed:24616510}.
-!- INTERACTION:
Q8IWY9:CDAN1; NbExp=3; IntAct=EBI-1055650, EBI-726307;
Q13111:CHAF1A; NbExp=4; IntAct=EBI-1055650, EBI-1020839;
Q13112:CHAF1B; NbExp=3; IntAct=EBI-1055650, EBI-1052944;
P84243:H3F3B; NbExp=4; IntAct=EBI-1055650, EBI-120658;
P54198:HIRA; NbExp=3; IntAct=EBI-1055650, EBI-372342;
P68431:HIST1H3D; NbExp=4; IntAct=EBI-1055650, EBI-79722;
Q09028:RBBP4; NbExp=2; IntAct=EBI-1055650, EBI-620823;
Q96HA7:TONSL; NbExp=3; IntAct=EBI-1055650, EBI-1052467;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12842904}.
-!- TISSUE SPECIFICITY: Highly expressed in testis and at lower levels
in colon, small intestine and thymus.
{ECO:0000269|PubMed:12842904}.
-!- PTM: Phosphorylated by TLK1 and TLK2.
{ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:20016786}.
-!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF279307; AAK82973.1; -; mRNA.
EMBL; AB104486; BAC87709.1; -; mRNA.
EMBL; CR457235; CAG33516.1; -; mRNA.
EMBL; AK001288; BAA91602.1; -; mRNA.
EMBL; AK001466; BAA91708.1; -; mRNA.
EMBL; AK223080; BAD96800.1; -; mRNA.
EMBL; AC022098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007726; AAH07726.1; -; mRNA.
EMBL; BC010014; AAH10014.1; -; mRNA.
EMBL; BC036521; AAH36521.1; -; mRNA.
CCDS; CCDS12306.1; -.
RefSeq; NP_060624.1; NM_018154.2.
UniGene; Hs.26516; -.
PDB; 5BNX; X-ray; 2.31 A; D=1-158.
PDB; 5BO0; X-ray; 2.91 A; D=1-158.
PDBsum; 5BNX; -.
PDBsum; 5BO0; -.
ProteinModelPortal; Q9NVP2; -.
SMR; Q9NVP2; -.
BioGrid; 120845; 60.
CORUM; Q9NVP2; -.
DIP; DIP-29242N; -.
IntAct; Q9NVP2; 37.
MINT; Q9NVP2; -.
STRING; 9606.ENSP00000263382; -.
iPTMnet; Q9NVP2; -.
PhosphoSitePlus; Q9NVP2; -.
BioMuta; ASF1B; -.
EPD; Q9NVP2; -.
MaxQB; Q9NVP2; -.
PaxDb; Q9NVP2; -.
PeptideAtlas; Q9NVP2; -.
PRIDE; Q9NVP2; -.
DNASU; 55723; -.
Ensembl; ENST00000263382; ENSP00000263382; ENSG00000105011.
GeneID; 55723; -.
KEGG; hsa:55723; -.
UCSC; uc002mye.4; human.
CTD; 55723; -.
DisGeNET; 55723; -.
EuPathDB; HostDB:ENSG00000105011.8; -.
GeneCards; ASF1B; -.
HGNC; HGNC:20996; ASF1B.
HPA; HPA054036; -.
MIM; 609190; gene.
neXtProt; NX_Q9NVP2; -.
OpenTargets; ENSG00000105011; -.
PharmGKB; PA134931112; -.
eggNOG; KOG3265; Eukaryota.
eggNOG; COG5137; LUCA.
GeneTree; ENSGT00390000004692; -.
HOGENOM; HOG000197425; -.
HOVERGEN; HBG105617; -.
InParanoid; Q9NVP2; -.
KO; K10753; -.
OMA; HINWEGC; -.
OrthoDB; EOG091G0K07; -.
PhylomeDB; Q9NVP2; -.
TreeFam; TF106429; -.
ChiTaRS; ASF1B; human.
GeneWiki; ASF1B; -.
GenomeRNAi; 55723; -.
PRO; PR:Q9NVP2; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105011; -.
CleanEx; HS_ASF1B; -.
ExpressionAtlas; Q9NVP2; baseline and differential.
Genevisible; Q9NVP2; HS.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; IDA:UniProtKB.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; IDA:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.60.40.1490; -; 1.
InterPro; IPR006818; ASF1-like.
InterPro; IPR036747; ASF1-like_sf.
PANTHER; PTHR12040; PTHR12040; 1.
Pfam; PF04729; ASF1_hist_chap; 1.
SUPFAM; SSF101546; SSF101546; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Chromatin regulator; Complete proteome;
Developmental protein; Differentiation; Nucleus; Phosphoprotein;
Reference proteome; Spermatogenesis; Transcription;
Transcription regulation.
CHAIN 1 202 Histone chaperone ASF1B.
/FTId=PRO_0000284015.
REGION 1 156 Interaction with histone H3.
{ECO:0000250}.
REGION 1 155 Interaction with CHAF1B.
MOD_RES 198 198 Phosphoserine; by TLK2.
{ECO:0000269|PubMed:20016786}.
MUTAGEN 36 36 D->A: Abolishes CDAN1 interaction.
{ECO:0000269|PubMed:22407294}.
MUTAGEN 37 37 D->A: Abolishes CDAN1 interaction.
{ECO:0000269|PubMed:22407294}.
CONFLICT 11 11 V -> A (in Ref. 4; BAA91602).
{ECO:0000305}.
CONFLICT 23 23 R -> Q (in Ref. 5; BAD96800).
{ECO:0000305}.
STRAND 3 11 {ECO:0000244|PDB:5BNX}.
STRAND 15 17 {ECO:0000244|PDB:5BNX}.
STRAND 22 32 {ECO:0000244|PDB:5BNX}.
STRAND 34 36 {ECO:0000244|PDB:5BNX}.
STRAND 38 45 {ECO:0000244|PDB:5BNX}.
HELIX 51 53 {ECO:0000244|PDB:5BNX}.
STRAND 54 62 {ECO:0000244|PDB:5BNX}.
STRAND 67 76 {ECO:0000244|PDB:5BNX}.
HELIX 81 83 {ECO:0000244|PDB:5BNX}.
HELIX 86 89 {ECO:0000244|PDB:5BNX}.
STRAND 90 101 {ECO:0000244|PDB:5BNX}.
STRAND 104 117 {ECO:0000244|PDB:5BNX}.
HELIX 120 124 {ECO:0000244|PDB:5BNX}.
HELIX 132 134 {ECO:0000244|PDB:5BNX}.
STRAND 135 139 {ECO:0000244|PDB:5BNX}.
STRAND 145 148 {ECO:0000244|PDB:5BNX}.
SEQUENCE 202 AA; 22434 MW; BD62F726610E3A70 CRC64;
MAKVSVLNVA VLENPSPFHS PFRFEISFEC SEALADDLEW KIIYVGSAES EEFDQILDSV
LVGPVPAGRH MFVFQADAPN PSLIPETDAV GVTVVLITCT YHGQEFIRVG YYVNNEYLNP
ELRENPPMKP DFSQLQRNIL ASNPRVTRFH INWDNNMDRL EAIETQDPSL GCGLPLNCTP
IKGLGLPGCI PGLLPENSMD CI


Related products :

Catalog number Product name Quantity
30-183 ASF1B is a member of the H3_H4 family of histone chaperone proteins and is similar to the anti-silencing function-1 gene in yeast. The encoded protein is the substrate of the tousled-like kinase famil 0.05 mg
ASGR2 ASF1B Gene ASF1 anti-silencing function 1 homolog B (S. cerevisiae)
201-20-0474 ASF1B{ASF1 silencing function 1 homolog B (S. cerevisiae)}rabbit.pAb 0.1ml
CSB-EL002206HU Human ASF1 anti-silencing function 1 homolog B (S. cerevisiae) (ASF1B) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL002206MO Mouse ASF1 anti-silencing function 1 homolog B (S. cerevisiae) (ASF1B) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL002206BO Bovine ASF1 anti-silencing function 1 homolog B (S. cerevisiae) (ASF1B) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
ASF1B_MOUSE ELISA Kit FOR Histone chaperone ASF1B; organism: Mouse; gene name: Asf1b 96T
CSB-EL002206HU Human Histone chaperone ASF1B(ASF1B) ELISA kit SpeciesHuman 96T
CSB-EL002206MO Mouse Histone chaperone ASF1B(ASF1B) ELISA kit SpeciesMouse 96T
CSB-EL002206BO Bovine Histone chaperone ASF1B(ASF1B) ELISA kit SpeciesBovine 96T
CSB-EL002206HU Human Histone chaperone ASF1B(ASF1B) ELISA kit 96T
CSB-EL002206MO Mouse Histone chaperone ASF1B(ASF1B) ELISA kit 96T
CSB-EL002206BO Bovine Histone chaperone ASF1B(ASF1B) ELISA kit 96T
orb80932 Human ASF1 Anti-Silencing Function Homolog A protein Proteins 5
ASF1B_BOVIN Bovine ELISA Kit FOR Histone chaperone ASF1B 96T
RPR-163 Recombinant Human ASF1 Anti-Silencing Function 1 Homolog B 5
RPR-682 Recombinant Human ASF1 Anti-Silencing Function 1 Homolog A 5
pro-682 Recombinant Human ASF1 Anti-Silencing Function 1 Homolog A 20
pro-682 Recombinant Human ASF1 Anti-Silencing Function 1 Homolog A 5
E14536h Human Anti Silencing Function 1 Homolog B ELISA Ki 96T
E14537h Human Anti Silencing Function 1 Homolog A ELISA Ki 96T
pro-682 Recombinant Human ASF1 Anti-Silencing Function 1 Homolog A 1mg
pro-1163 Recombinant Human ASF1 Anti-Silencing Function 1 Homolog B 5
pro-682 Recombinant Human ASF1 Anti-Silencing Function 1 Homolog A ASF1A 1mg
pro-1163 Recombinant Human ASF1 Anti-Silencing Function 1 Homolog B 20


 

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