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

Helicase-like transcription factor (EC 2.3.2.27) (EC 3.6.4.-) (RING-type E3 ubiquitin transferase HLTF) (RUSH-1) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3) (Sucrose nonfermenting protein 2-like 3)

 HLTF_RABIT              Reviewed;        1005 AA.
Q95216; Q95217;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 119.
RecName: Full=Helicase-like transcription factor;
EC=2.3.2.27;
EC=3.6.4.-;
AltName: Full=RING-type E3 ubiquitin transferase HLTF {ECO:0000305};
AltName: Full=RUSH-1;
AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3;
AltName: Full=Sucrose nonfermenting protein 2-like 3;
Name=HLTF; Synonyms=RUSH1, SMARCA3;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INDUCTION, AND TISSUE
SPECIFICITY.
STRAIN=New Zealand white; TISSUE=Endometrium;
PubMed=8923460; DOI=10.1210/mend.10.11.8923460;
Hayward-Lester A., Hewetson A., Beale E.G., Oefner P.J., Doris P.A.,
Chilton B.S.;
"Cloning, characterization, and steroid-dependent posttranscriptional
processing of RUSH-1 alpha and beta, two uteroglobin promoter-binding
proteins.";
Mol. Endocrinol. 10:1335-1349(1996).
[2]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=9370258; DOI=10.1016/S0378-1119(97)00305-3;
Robinson C.A., Hayward-Lester A., Hewetson A., Oefner P.J.,
Doris P.A., Chilton B.S.;
"Quantification of alternatively spliced RUSH mRNA isoforms by QRT-PCR
and IP-RP-HPLC analysis: a new approach to measuring regulated
splicing efficiency.";
Gene 198:1-4(1997).
[3]
TISSUE SPECIFICITY.
PubMed=10859255; DOI=10.1095/biolreprod63.1.156;
Rendon A., Hewetson A., Chilton B.S., Lee V.H.;
"Expression of RUSH transcription factors in developing and adult
rabbit gonads.";
Biol. Reprod. 63:156-164(2000).
[4]
FUNCTION, AND INTERACTION WITH ATP11B.
PubMed=11058586; DOI=10.1074/jbc.M004231200;
Mansharamani M., Hewetson A., Chilton B.S.;
"Cloning and characterization of an atypical type IV P-type ATPase
that binds to the RING motif of RUSH transcription factors.";
J. Biol. Chem. 276:3641-3649(2001).
[5]
DNA-BINDING, INTERACTION WITH GATA4, INDUCTION, AND TISSUE
SPECIFICITY.
PubMed=12198246; DOI=10.1210/me.2002-0064;
Hewetson A., Hendrix E.C., Mansharamani M., Lee V.H., Chilton B.S.;
"Identification of the RUSH consensus-binding site by cyclic
amplification and selection of targets: demonstration that RUSH
mediates the ability of prolactin to augment progesterone-dependent
gene expression.";
Mol. Endocrinol. 16:2101-2112(2002).
[6]
DNA-BINDING, AND FUNCTION.
PubMed=12890680; DOI=10.1074/jbc.M303921200;
Hewetson A., Chilton B.S.;
"An Sp1-NF-Y/progesterone receptor DNA binding-dependent mechanism
regulates progesterone-induced transcriptional activation of the
rabbit RUSH/SMARCA3 gene.";
J. Biol. Chem. 278:40177-40185(2003).
[7]
INTERACTION WITH EGR1, PHOSPHORYLATION, AND FUNCTION.
PubMed=15306550; DOI=10.1095/biolreprod.104.031435;
Hewetson A., Moore S.L., Chilton B.S.;
"Prolactin signals through RUSH/SMARCA3 in the absence of a physical
association with Stat5a.";
Biol. Reprod. 71:1907-1912(2004).
[8]
FUNCTION.
PubMed=18631131; DOI=10.1042/BST0360632;
Chilton B.S., Hewetson A.;
"Progesterone regulation of RUSH/SMARCA3/HLTF includes DNA looping.";
Biochem. Soc. Trans. 36:632-636(2008).
[9]
INTERACTION WITH ATP11B, AND MUTAGENESIS OF PRO-767; VAL-768; ILE-769;
HIS-771; ALA-792 AND LYS-793.
PubMed=18584949; DOI=10.1016/j.mce.2008.05.007;
Hewetson A., Wright-Pastusek A.E., Helmer R.A., Wesley K.A.,
Chilton B.S.;
"Conservation of inter-protein binding sites in RUSH and RFBP, an
ATP11B isoform.";
Mol. Cell. Endocrinol. 292:79-86(2008).
[10]
INTERACTION WITH EGR1 AND REL, DNA-BINDING, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=18174357; DOI=10.1210/me.2007-0432;
Hewetson A., Chilton B.S.;
"Progesterone-dependent deoxyribonucleic acid looping between
RUSH/SMARCA3 and Egr-1 mediates repression by c-Rel.";
Mol. Endocrinol. 22:813-822(2008).
[11]
SUBCELLULAR LOCATION, INDUCTION, AND PHOSPHORYLATION BY JAK2.
PubMed=20562009; DOI=10.1016/j.mce.2010.05.010;
Helmer R.A., Panchoo M., Dertien J.S., Bhakta S.M., Hewetson A.,
Chilton B.S.;
"Prolactin-induced Jak2 phosphorylation of RUSH: a key element in
Jak/RUSH signaling.";
Mol. Cell. Endocrinol. 325:143-149(2010).
[12]
FUNCTION IN SCGB1A1 PROMOTER BINDING, AND PHOSPHORYLATION AT TYR-195.
PubMed=21457752; DOI=10.1016/j.mce.2011.03.009;
Helmer R.A., Dertien J.S., Chilton B.S.;
"Prolactin induces Jak2 phosphorylation of RUSHY195.";
Mol. Cell. Endocrinol. 338:79-83(2011).
-!- FUNCTION: Has both helicase and E3 ubiquitin ligase activities.
Possesses intrinsic ATP-dependent nucleosome-remodeling activity.
This activity may be required for transcriptional activation or
repression of specific target promoters (By similarity). These may
include the SERPINE1, to which this protein can bind directly.
Mediates repression by c-Rel through a DNA-looping mechanism.
Plays a role in error-free postreplication repair (PRR) of damaged
DNA and maintains genomic stability through acting as a ubiquitin
ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound
PCNA (By similarity). Transcriptional regulator that mediates the
ability of prolactin to augment progesterone-dependent
transcription of the SCGB1A1/uteroglobin gene through a bipartite
progesterone receptor half-site/overlapping Y-box combination (-
38/-26) where progesterone activation is attenuated by nuclear
factor Y binding. Regulation also involves two GC-rich sequences
in the proximal promoter (positions -162/+90) and a RUSH/SMARCA3
site (positions -616/-611) in the 5'-untranslated region.
{ECO:0000250, ECO:0000269|PubMed:11058586,
ECO:0000269|PubMed:12890680, ECO:0000269|PubMed:15306550,
ECO:0000269|PubMed:18174357, ECO:0000269|PubMed:18631131,
ECO:0000269|PubMed:21457752}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with SP1 and SP3 independently of DNA; the
interaction with these transcriptional factors may be required for
basal transcription of target genes (By similarity). Interacts
(via the RING-finger) with isoform RFBP of ATP11B. Progesterone-
dependent isoform 1 interacts with EGR1; the interaction requires
prior binding to DNA and represses c-Rel via a DNA looping
mechanism. Interacts with GATA4. Interacts with PCNA; the
interaction promotes polyubiquitination of PCNA through
association with the UBE2B-RAD18 and UBE2V2-UBE2N ubiquitin ligase
complexes. Interacts with RAD18, SHPRH, UBE2V2 and UBE2N (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus,
nucleoplasm. Note=Cytoplasmic and nuclear localization in the
presence of prolactin. Nuclear localization is stimulated by
progesterone.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=RUSH 1-alpha;
IsoId=Q95216-1; Sequence=Displayed;
Note=Major isoform in progesterone-dominant endometrium.;
Name=2; Synonyms=RUSH 1-beta;
IsoId=Q95216-2; Sequence=VSP_012923, VSP_012924;
Note=Truncated, estrogen-dependent isoform.;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed preferentially in
bladder, cervix, diaphragm, duodenum, epididymis, heart, kidney,
liver, lung, ovary (granulosa cells), prostate, spleen, testis
(predominantly in the Sertoli cells of the seminiferous tubules)
and vagina. Isoform 2 is expressed preferentially in lactating
mammary gland and uterine endometrium.
{ECO:0000269|PubMed:10859255, ECO:0000269|PubMed:12198246,
ECO:0000269|PubMed:8923460, ECO:0000269|PubMed:9370258}.
-!- INDUCTION: Isoform RUSH 1-alpha expression is increased by
progesterone and decreased by estradiol. Progesterone induction is
increased in the presence of prolactin. Isoform RUSH 1-beta/RFBP
expression is increased by estrogen and decreased by progesterone.
{ECO:0000269|PubMed:12198246, ECO:0000269|PubMed:20562009,
ECO:0000269|PubMed:8923460}.
-!- PTM: Phosphorylated on serine, threonine, and tyrosine residues.
Tyr-195 phosphorylation is catalyzed by JAK2 in response to
prolactin treatment. It is required for DNA binding.
{ECO:0000269|PubMed:15306550, ECO:0000269|PubMed:20562009,
ECO:0000269|PubMed:21457752}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U66564; AAC18656.1; -; mRNA.
EMBL; U66565; AAC48693.1; -; mRNA.
RefSeq; NP_001075845.1; NM_001082376.1. [Q95216-2]
RefSeq; NP_001108200.1; NM_001114728.1. [Q95216-1]
UniGene; Ocu.2614; -.
ProteinModelPortal; Q95216; -.
SMR; Q95216; -.
STRING; 9986.ENSOCUP00000003055; -.
iPTMnet; Q95216; -.
PRIDE; Q95216; -.
GeneID; 100009232; -.
KEGG; ocu:100009232; -.
CTD; 6596; -.
eggNOG; KOG1001; Eukaryota.
eggNOG; COG0553; LUCA.
HOGENOM; HOG000172619; -.
HOVERGEN; HBG079192; -.
InParanoid; Q95216; -.
KO; K15711; -.
UniPathway; UPA00143; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00079; HELICc; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014905; HIRAN.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000330; SNF2_N.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF08797; HIRAN; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00910; HIRAN; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF52540; SSF52540; 4.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; ATP-binding; Chromatin regulator;
Complete proteome; Cytoplasm; DNA-binding; Helicase; Hydrolase;
Isopeptide bond; Metal-binding; Methylation; Multifunctional enzyme;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transferase; Ubl conjugation; Ubl conjugation pathway;
Zinc; Zinc-finger.
CHAIN 1 1005 Helicase-like transcription factor.
/FTId=PRO_0000056186.
DOMAIN 427 603 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 834 999 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DNA_BIND 38 287 {ECO:0000250}.
NP_BIND 294 301 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
ZN_FING 757 798 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 767 772 Required for interaction with the RFBP
isoform of ATP11B.
REGION 791 796 Required for interaction with the RFBP
isoform of ATP11B.
REGION 922 1005 Interaction with SP1 and SP3.
{ECO:0000250}.
MOTIF 554 557 DEGH box.
MOD_RES 27 27 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q14527}.
MOD_RES 195 195 Phosphotyrosine; by JAK2.
{ECO:0000269|PubMed:21457752}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000250|UniProtKB:Q14527}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000250|UniProtKB:Q14527}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000250|UniProtKB:Q14527}.
MOD_RES 733 733 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14527}.
CROSSLNK 112 112 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q14527}.
CROSSLNK 211 211 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q14527}.
VAR_SEQ 832 836 INALM -> RFLSC (in isoform 2).
{ECO:0000303|PubMed:8923460}.
/FTId=VSP_012923.
VAR_SEQ 837 1005 Missing (in isoform 2).
{ECO:0000303|PubMed:8923460}.
/FTId=VSP_012924.
MUTAGEN 767 767 P->S,T: Abolishes binding to the RFBP
isoform of ATP11B.
{ECO:0000269|PubMed:18584949}.
MUTAGEN 768 768 V->R: Abolishes binding to the RFBP
isoform of ATP11B.
{ECO:0000269|PubMed:18584949}.
MUTAGEN 769 769 I->M,P: Abolishes binding to the RFBP
isoform of ATP11B.
{ECO:0000269|PubMed:18584949}.
MUTAGEN 771 771 H->D,K: Abolishes binding to the RFBP
isoform of ATP11B.
{ECO:0000269|PubMed:18584949}.
MUTAGEN 792 792 A->Q: Abolishes binding to the RFBP
isoform of ATP11B.
{ECO:0000269|PubMed:18584949}.
MUTAGEN 793 793 K->P: Abolishes binding to the RFBP
isoform of ATP11B.
{ECO:0000269|PubMed:18584949}.
SEQUENCE 1005 AA; 113582 MW; C741E7117D6BD807 CRC64;
MSWMFKRDPV WKYLQTVQYG VHGNFSRLSY PTFFPRFEFQ DIIPPDDFLT SDEELDSVLF
GTLRGHVVGL RYYTGVVNNN EMVALQREPN NPYDKNAIKV NNVNGNQVGY LKKELAAALA
YIMDNKLAQI EGVVPYGANN AFTMPLQMTF WGKEENRKAV LDQLKKHGFK LGPAPKTLGF
SLESGWGSGR AGPSYSMPVH AAIQMTTEQL KTEFDKLFED LKEDDKTQEM EPAEAVETPL
LPHQKQALAW MVSRENSREL PPFWELRNDL YYNTITNFSE KDQPENVHGG ILADDMGLGK
TLTAIAVILT NFHDGKPLPV ERMKKNQVKK ECNSSESDKP GRKDTIKKTD GLSKEGSRYS
EEPSISDVKK NKYSMSELSS SQPKRKKIAV QYIESSDSEE IEISELPQKM KGKLKNVQSE
TKRVKVGPSK IKEDTAFACA LTSSASTTTK KILKKGASAQ RVQRKLMFEE RPRTTLIICP
LSVLSNWIDQ FGQHIKSDVH LNFYVYYGPD RIRDPALLSK QDIVLTTYNI LTHDYGTKGD
SPLHSIRWLR VILDEGHAIR NPNAQQTKAV LDLEAERRWV LTGTPIQNSL KDLWSLLSFL
KLKPFVDREW WHRTIQRPVT MGDEGGLRRL QSLIKNITLR RTKTSKIKGK PVLELPERPV
FIQHITLSDE ERKIYQSVKS EGKATIGRYF NEGTVLAHYA DVLGLLLRLR QICCHTHLLT
NTVSSSGPSG NDTPEELRKK LIKKMKLILS SGSDEECAIC LDSLTVPVIT HCAHVFCKPC
ICQCIQNEQP HAKCPLCRND IHGDNLLECP PEELACDSEK KSNMEWTSSS KINALMHALI
DLRTKNPNIK SLVVSQFTTF LSLIETPLKA SGFVFTRLDG SMAQKKRVES IQCFQNTEAG
SPTIMLLSLK AGGVGLNLCA ASRVFLMDPA WNPAAEDQRF DRCHRLGQKQ EVIITKFIVK
DSVEENMLKI QNTKRELAAG AFGTKKNANE MKQAKINEIR TLIDL


Related products :

Catalog number Product name Quantity
EIAAB38782 Mouse,mSnf2h,Mus musculus,Smarca5,Snf2h,Sucrose nonfermenting protein 2 homolog,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
18-272-196662 SMARCA3 - Rabbit polyclonal to SMARCA3; EC 3.6.1.-; SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3; Sucrose nonfermenting protein 2-like 3; DNA-binding p 0.05 mg
EIAAB38733 Harp,HepA-related protein,Rat,Rattus norvegicus,Smarcal1,Sucrose nonfermenting protein 2-like 1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
EIAAB38735 Bos taurus,Bovine,HARP,HepA-related protein,SMARCAL1,Sucrose nonfermenting protein 2-like 1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
EIAAB38732 Harp,HepA-related protein,mharp,Mouse,Mus musculus,Smarcal1,Sucrose nonfermenting protein 2-like 1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
EIAAB38734 HARP,HepA-related protein,hHARP,Homo sapiens,Human,SMARCAL1,Sucrose nonfermenting protein 2-like 1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
EIAAB38783 Homo sapiens,hSNF2H,Human,SMARCA5,SNF2H,Sucrose nonfermenting protein 2 homolog,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin A5,SWI_SNF-related matrix-associated actin-depe
20-372-60078 SWI_SNF related. matrix associated. actin dependent regulator of chromatin. subfamily a. member 4 (SMARCA4) - Mouse monoclonal anti-human SMARCA4 antibody; EC 3.6.1.-; ATP-dependent helicase SMARCA4; 0.1 mg
18-003-43477 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 - BRG1-associated factor 57 Polyclonal 0.05 mg Aff Pur
18-272-195641 SMARCA2 - Rabbit polyclonal to SMARCA2; EC 3.6.1.-; ATP-dependent helicase SMARCA2; SNF2-alpha; SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2; hBRM Poly 0.1 ml
18-272-195642 SMARCA2 - Rabbit polyclonal to SMARCA2; EC 3.6.1.-; ATP-dependent helicase SMARCA2; SNF2-alpha; SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2; hBRM Poly 0.1 ml
EIAAB38861 ATP-dependent helicase 1,hHEL1,Homo sapiens,Human,KIAA1122,SMARCAD1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD_H box 1
18-003-43138 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3 - 60 kDa BRG-1_Brm-associated factor subunit C; BRG1-associated factor 60C Polyclonal 0.05 mg Aff Pur
18-003-43476 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2 - 60 kDa BRG-1_Brm-associated factor subunit B; BRG1-associated factor 60B Polyclonal 0.05 mg Aff Pur
EIAAB38867 60 kDa BRG-1_Brm-associated factor subunit B,BAF60B,Bos taurus,Bovine,BRG1-associated factor 60B,SMARCD2,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2
18-003-43154 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related - SMARCE1-related protein; HMG domain protein HMG20B; Structural DNA-binding protein BRAF35; BRCA2 0.05 mg Aff Pur
H3860 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related (HMG20B), Bovine, ELISA Kit 96T
H3862 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related (HMG20B), Mouse, ELISA Kit 96T
H3861 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related (HMG20B), Human, ELISA Kit 96T
CSB-EL021809RA Rat SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 2 (SMARCD2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL021801RA Rat SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4) ELISA kit, Species Rat, Sample Type serum, plasma 96T
H3855 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2 (SMARCD2), Rat, ELISA Kit 96T
60078 IgG,SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4) 0.1 mg
SMCA5_HUMAN Human ELISA Kit FOR SWI per SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 96T
SMCE1_HUMAN Human ELISA Kit FOR SWI per SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 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