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

RNA polymerase-associated protein RTF1 homolog

 RTF1_HUMAN              Reviewed;         710 AA.
Q92541; Q96BX6;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 4.
18-JUL-2018, entry version 145.
RecName: Full=RNA polymerase-associated protein RTF1 homolog;
Name=RTF1; Synonyms=KIAA0252;
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 GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-710.
TISSUE=Brain;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-710.
TISSUE=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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, 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).
[7]
FUNCTION.
PubMed=19345177; DOI=10.1016/j.stem.2009.03.009;
Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M.,
Heninger A.K., de Vries I., Kittler R., Junqueira M., Shevchenko A.,
Schulz H., Hubner N., Doss M.X., Sachinidis A., Hescheler J.,
Iacone R., Anastassiadis K., Stewart A.F., Pisabarro M.T.,
Caldarelli A., Poser I., Theis M., Buchholz F.;
"A genome-scale RNAi screen for Oct4 modulators defines a role of the
Paf1 complex for embryonic stem cell identity.";
Cell Stem Cell 4:403-415(2009).
[8]
IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX,
AND FUNCTION OF THE PAF1 COMPLEX.
PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
Kim J., Guermah M., Roeder R.G.;
"The human PAF1 complex acts in chromatin transcription elongation
both independently and cooperatively with SII/TFIIS.";
Cell 140:491-503(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-650 AND SER-697,
AND 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).
[10]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND THR-55, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-650; SER-655
AND SER-697, 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).
[13]
STRUCTURE BY NMR OF 347-482.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the plus-3 domain of human KIAA0252 protein.";
Submitted (JUN-2006) to the PDB data bank.
[14]
STRUCTURE BY NMR OF 353-484, DOMAIN PLUS3, DNA-BINDING, AND
MUTAGENESIS OF ARG-401; GLU-410; ARG-429; GLN-434 AND ARG-435.
PubMed=18184592; DOI=10.1016/j.str.2007.10.018;
de Jong R.N., Truffault V., Diercks T., Ab E., Daniels M.A.,
Kaptein R., Folkers G.E.;
"Structure and DNA binding of the human Rtf1 Plus3 domain.";
Structure 16:149-159(2008).
-!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
functions during transcription by RNA polymerase II and is
implicated in regulation of development and maintenance of
embryonic stem cell pluripotency. PAF1C associates with RNA
polymerase II through interaction with POLR2A CTD non-
phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and
is involved in transcriptional elongation, acting both
indepentently and synergistically with TCEA1 and in cooperation
with the DSIF complex and HTATSF1. PAF1C is required for
transcription of Hox and Wnt target genes. PAF1C is involved in
hematopoiesis and stimulates transcriptional activity of
KMT2A/MLL1; it promotes leukemogenesis through association with
KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9
and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone
modifications such as ubiquitination of histone H2B and
methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the
RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme
UBE2A or UBE2B to chromatin which mediate monoubiquitination of
'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
ubiquitination is proposed to be coupled to transcription. PAF1C
is involved in mRNA 3' end formation probably through association
with cleavage and poly(A) factors. In case of infection by
influenza A strain H3N2, PAF1C associates with viral NS1 protein,
thereby regulating gene transcription. Binds single-stranded DNA.
Required for maximal induction of heat-shock genes. Required for
the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes
involved in stem cell pluripotency; this function is synergistic
with CXXC1 indicative for an involvement of a SET1 complex (By
similarity). {ECO:0000250, ECO:0000269|PubMed:19345177,
ECO:0000269|PubMed:20178742}.
-!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73,
PAF1, LEO1, CTR9, RTF1 and WDR61; the association of RTF1 appears
to be less stable than that of other subunits. At least in HeLa
cells a N-terminal shorter form of RTF1 is also found in the
complex (PubMed:20178742). The PAF1 complex interacts with PHF5A
(By similarity). {ECO:0000250|UniProtKB:A2AQ19,
ECO:0000269|PubMed:20178742}.
-!- INTERACTION:
Q6P1J9:CDC73; NbExp=12; IntAct=EBI-1055239, EBI-930143;
Q8N7H5:PAF1; NbExp=16; IntAct=EBI-1055239, EBI-2607770;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
-!- DOMAIN: The Plus3 domain mediates single-stranded DNA-binding.
{ECO:0000269|PubMed:18184592}.
-!- CAUTION: It is uncertain whether Met-1 or Met-41 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH15052.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA13382.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={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; AC087721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D87440; BAA13382.2; ALT_INIT; mRNA.
EMBL; BC015052; AAH15052.1; ALT_INIT; mRNA.
CCDS; CCDS32200.2; -.
RefSeq; NP_055953.3; NM_015138.4.
UniGene; Hs.511096; -.
PDB; 2BZE; NMR; -; A=353-484.
PDB; 2DB9; NMR; -; A=347-482.
PDB; 3U1U; X-ray; 1.80 A; A/B=347-482.
PDB; 4L1P; X-ray; 2.12 A; A/B=353-484.
PDB; 4L1U; X-ray; 2.42 A; A/B/C/D/E/F=353-484.
PDBsum; 2BZE; -.
PDBsum; 2DB9; -.
PDBsum; 3U1U; -.
PDBsum; 4L1P; -.
PDBsum; 4L1U; -.
ProteinModelPortal; Q92541; -.
SMR; Q92541; -.
BioGrid; 116780; 40.
IntAct; Q92541; 17.
MINT; Q92541; -.
STRING; 9606.ENSP00000374280; -.
iPTMnet; Q92541; -.
PhosphoSitePlus; Q92541; -.
BioMuta; RTF1; -.
DMDM; 313104316; -.
EPD; Q92541; -.
MaxQB; Q92541; -.
PaxDb; Q92541; -.
PeptideAtlas; Q92541; -.
PRIDE; Q92541; -.
ProteomicsDB; 75301; -.
Ensembl; ENST00000389629; ENSP00000374280; ENSG00000137815.
GeneID; 23168; -.
KEGG; hsa:23168; -.
UCSC; uc001zny.3; human.
CTD; 23168; -.
DisGeNET; 23168; -.
EuPathDB; HostDB:ENSG00000137815.14; -.
GeneCards; RTF1; -.
H-InvDB; HIX0012153; -.
HGNC; HGNC:28996; RTF1.
HPA; HPA006714; -.
MIM; 611633; gene.
neXtProt; NX_Q92541; -.
OpenTargets; ENSG00000137815; -.
PharmGKB; PA134961778; -.
eggNOG; KOG2402; Eukaryota.
eggNOG; COG5296; LUCA.
GeneTree; ENSGT00390000012493; -.
HOGENOM; HOG000231764; -.
HOVERGEN; HBG057331; -.
InParanoid; Q92541; -.
KO; K15178; -.
OMA; SGCKSAV; -.
OrthoDB; EOG091G1817; -.
PhylomeDB; Q92541; -.
TreeFam; TF321360; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
ChiTaRS; RTF1; human.
EvolutionaryTrace; Q92541; -.
GeneWiki; RTF1; -.
GenomeRNAi; 23168; -.
PMAP-CutDB; Q92541; -.
PRO; PR:Q92541; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000137815; -.
CleanEx; HS_RTF1; -.
ExpressionAtlas; Q92541; baseline and differential.
Genevisible; Q92541; HS.
GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IBA:GO_Central.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0001076; F:transcription factor activity, RNA polymerase II transcription factor binding; IBA:GO_Central.
GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
GO; GO:0080182; P:histone H3-K4 trimethylation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0019827; P:stem cell population maintenance; IDA:UniProtKB.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 2.170.260.30; -; 1.
InterPro; IPR004343; Plus-3_dom.
InterPro; IPR036128; Plus3-like_sf.
InterPro; IPR031102; Rtf1.
PANTHER; PTHR13115; PTHR13115; 1.
Pfam; PF03126; Plus-3; 1.
SMART; SM00719; Plus3; 1.
SUPFAM; SSF159042; SSF159042; 1.
PROSITE; PS51360; PLUS3; 1.
1: Evidence at protein level;
3D-structure; Activator; Coiled coil; Complete proteome; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Wnt signaling pathway.
CHAIN 1 710 RNA polymerase-associated protein RTF1
homolog.
/FTId=PRO_0000255936.
DOMAIN 353 484 Plus3. {ECO:0000255|PROSITE-
ProRule:PRU00693}.
COILED 526 560 {ECO:0000255}.
COMPBIAS 10 18 Poly-Ala.
COMPBIAS 135 173 Ser-rich.
COMPBIAS 174 345 Glu-rich.
COMPBIAS 214 307 Lys-rich.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 55 55 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 655 655 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 697 697 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MUTAGEN 401 401 R->E: Loss of binding to single-stranded
DNA. {ECO:0000269|PubMed:18184592}.
MUTAGEN 410 410 E->K: Reduced binding to single-stranded
DNA. {ECO:0000269|PubMed:18184592}.
MUTAGEN 429 429 R->E: Loss of binding to single-stranded
DNA. {ECO:0000269|PubMed:18184592}.
MUTAGEN 434 434 Q->A: Reduced binding to single-stranded
DNA. {ECO:0000269|PubMed:18184592}.
MUTAGEN 435 435 R->E: Loss of binding to single-stranded
DNA. {ECO:0000269|PubMed:18184592}.
HELIX 356 360 {ECO:0000244|PDB:3U1U}.
STRAND 362 364 {ECO:0000244|PDB:2BZE}.
HELIX 366 372 {ECO:0000244|PDB:3U1U}.
STRAND 373 377 {ECO:0000244|PDB:2BZE}.
HELIX 378 382 {ECO:0000244|PDB:3U1U}.
STRAND 386 392 {ECO:0000244|PDB:3U1U}.
STRAND 395 397 {ECO:0000244|PDB:2BZE}.
STRAND 399 417 {ECO:0000244|PDB:3U1U}.
STRAND 420 430 {ECO:0000244|PDB:3U1U}.
STRAND 433 438 {ECO:0000244|PDB:3U1U}.
HELIX 439 441 {ECO:0000244|PDB:3U1U}.
HELIX 449 462 {ECO:0000244|PDB:3U1U}.
HELIX 469 478 {ECO:0000244|PDB:3U1U}.
SEQUENCE 710 AA; 80313 MW; 54CC014655AA22B8 CRC64;
MRGRLCVGRA AAAAAAVAVP LAGGQEGSPG GGRRGSRGTT MVKKRKGRVV IDSDTEDSGS
DENLDQELLS LAKRKRSDSE EKEPPVSQPA ASSDSETSDS DDEWTFGSNK NKKKGKARKI
EKKGTMKKQA NKTASSGSSD KDSSAESSAP EEGEVSDSDS NSSSSSSDSD SSSEDEEFHD
GYGEDLMGDE EDRARLEQMT EKEREQELFN RIEKREVLKR RFEIKKKLKT AKKKEKKEKK
KKQEEEQEKK KLTQIQESQV TSHNKERRSK RDEKLDKKSQ AMEELKAERE KRKNRTAELL
AKKQPLKTSE VYSDDEEEEE DDKSSEKSDR SSRTSSSDEE EEKEEIPPKS QPVSLPEELN
RVRLSRHKLE RWCHMPFFAK TVTGCFVRIG IGNHNSKPVY RVAEITGVVE TAKVYQLGGT
RTNKGLQLRH GNDQRVFRLE FVSNQEFTES EFMKWKEAMF SAGMQLPTLD EINKKELSIK
EALNYKFNDQ DIEEIVKEKE RFRKAPPNYA MKKTQLLKEK AMAEDLGDQD KAKQIQDQLN
ELEERAEALD RQRTKNISAI SYINQRNREW NIVESEKALV AESHNMKNQQ MDPFTRRQCK
PTIVSNSRDP AVQAAILAQL NAKYGSGVLP DAPKEMSKGQ GKDKDLNSKS ASDLSEDLFK
VHDFDVKIDL QVPSSESKAL AITSKAPPAK DGAPRRSLNL EDYKKRRGLI


Related products :

Catalog number Product name Quantity
RTF1 RTF1 Gene Rtf1, Paf1_RNA polymerase II complex component, homolog (S. cerevisiae)
CSB-EL020564HU Human RNA polymerase-associated protein RTF1 homolog(RTF1) ELISA kit SpeciesHuman 96T
CSB-EL020564MO Mouse RNA polymerase-associated protein RTF1 homolog(RTF1) ELISA kit SpeciesMouse 96T
CSB-EL020564MO Mouse RNA polymerase-associated protein RTF1 homolog(RTF1) ELISA kit 96T
EIAAB36374 Mouse,Mus musculus,RNA polymerase-associated protein RTF1 homolog,Rtf1
G8246 RNA polymerase-associated protein RTF1 homolog (RTF1), Mouse, ELISA Kit 96T
G8245 RNA polymerase-associated protein RTF1 homolog (RTF1), Human, ELISA Kit 96T
CSB-EL020564HU Human RNA polymerase-associated protein RTF1 homolog(RTF1) ELISA kit 96T
RTF1_MOUSE ELISA Kit FOR RNA polymerase-associated protein RTF1 homolog; organism: Mouse; gene name: Rtf1 96T
EIAAB36373 Homo sapiens,Human,KIAA0252,RNA polymerase-associated protein RTF1 homolog,RTF1
201-20-5053 RTF1{Rtf1, Paf1_RNA polymerase II complex component, homolog (S. cerevisiae)}rabbit.pAb 0.2ml
CSB-EL020564MO Mouse Rtf1, Paf1_RNA polymerase II complex component, homolog (S. cerevisiae) (RTF1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL020564HU Human Rtf1, Paf1_RNA polymerase II complex component, homolog (S. cerevisiae) (RTF1) ELISA kit, Species Human, Sample Type serum, plasma 96T
STRAB_MOUSE Mouse ELISA Kit FOR RNA polymerase-associated protein RTF1 homolog 96T
E0699m Mouse ELISA Kit FOR RNA polymerase-associated protein RTF1 homolog 96T
GS-1927a Rtf1, Paf1_RNA polymerase II complex component, homolog (S. cerevisiae) primary antibody, Host: Rabbit 200ul
A4529 RTF1 Primary Antibody, RTF1, Species: Human Recombinant Protein Source: Rabbit Polyclonal 100ug
CSB-PA020564GA01HU Rabbit anti-human Rtf1, Paf1_RNA polymerase II complex component, homolog (S. cerevisiae) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA020564GA01HU Rabbit anti-human Rtf1, Paf1_RNA polymerase II complex component, homolog (S. cerevisiae) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
E3496h Human RTF1, Paf1_RNA Polymerase II Complex Compone 96T
EIAAB31781 DNA polymerase eta,Mouse,Mus musculus,Polh,RAD30 homolog A,Rad30a,Xeroderma pigmentosum variant type protein homolog,Xpv
EIAAB35821 DNA-directed RNA polymerase III subunit RPC5,Mouse,Mus musculus,Polr3e,RNA polymerase III subunit 5,RNA polymerase III subunit C5,Sex-lethal interactor homolog,Sin
H00023168-P01-25 RTF1 (Human) Recombinant Protein (P01) 25 ug
5244 Protein,RNA polymerase transcriptional regulation mediator, subunit 6 homolog 1 mg
orb90215 Pfu DNA Polymerase protein Pfu DNA Polymerase is thermo-stable enzyme having Mw of about 90kDa. Pfu DNA Polymerase is derived from E.coli that and cloned from Pyrococcus furiosus strain Vc1 DSM3638. P 100 U


 

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