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

DBIRD complex subunit ZNF326 (Zinc finger protein 326) (Zinc finger protein interacting with mRNPs) (Zinc finger protein-associated with nuclear matrix of 75 kDa)

 ZN326_MOUSE             Reviewed;         580 AA.
O88291; Q05DP5; Q3TRI9; Q3UJI3; Q8BSJ5; Q8K1X9; Q9CYG9;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 130.
RecName: Full=DBIRD complex subunit ZNF326;
AltName: Full=Zinc finger protein 326;
AltName: Full=Zinc finger protein interacting with mRNPs;
AltName: Full=Zinc finger protein-associated with nuclear matrix of 75 kDa;
Name=Znf326; Synonyms=Zan75, Zfp326, Zird;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9809746; DOI=10.1089/dna.1998.17.849;
Lee J.-Y., Kambe M., Hayashi M., Takenaga K.;
"Cloning and characterization of a novel zinc finger protein that
associates with nuclear matrix.";
DNA Cell Biol. 17:849-858(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Thymus, and Wolffian duct;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-277 (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
[4]
FUNCTION, BIPARTITE NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=10798446; DOI=10.1089/104454900314492;
Lee J.-Y., Nakane Y., Koshikawa N., Nakayama K., Hayashi M.,
Takenaga K.;
"Characterization of a zinc finger protein ZAN75: nuclear localization
signal, transcriptional activator activity, and expression during
neuronal differentiation of P19 cells.";
DNA Cell Biol. 19:227-234(2000).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-270, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-235, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Core component of the DBIRD complex, a multiprotein
complex that acts at the interface between core mRNP particles and
RNA polymerase II (RNAPII) and integrates transcript elongation
with the regulation of alternative splicing: the DBIRD complex
affects local transcript elongation rates and alternative splicing
of a large set of exons embedded in (A + T)-rich DNA regions (By
similarity). May also play a role in neuronal differentiation.
Able to bind DNA and activate expression in vitro. {ECO:0000250,
ECO:0000269|PubMed:10798446}.
-!- SUBUNIT: Component of the DBIRD complex. Interacts with CCAR2; the
interaction is direct (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:10798446,
ECO:0000269|PubMed:9809746}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O88291-1; Sequence=Displayed;
Name=2;
IsoId=O88291-2; Sequence=VSP_014957;
Note=No experimental confirmation available.;
Name=3;
IsoId=O88291-3; Sequence=VSP_014958, VSP_014959;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues.
Highly expressed in neuronal tissues such as brain and neural
tube. {ECO:0000269|PubMed:10798446, ECO:0000269|PubMed:9809746}.
-!- DEVELOPMENTAL STAGE: Weakly expressed during E9.5 and E10.5,
expressed at highest level in E11.5 and gradually decreases
thereafter. During the cell cycle, it is weakly expressed in G0
and G1 phases. It increases during G1, S, G2 and M phases.
{ECO:0000269|PubMed:10798446, ECO:0000269|PubMed:9809746}.
-!- INDUCTION: Upon retinoic acid treatment.
{ECO:0000269|PubMed:10798446}.
-!- SIMILARITY: Belongs to the AKAP95 family. {ECO:0000255|PROSITE-
ProRule:PRU01140}.
-!- SEQUENCE CAUTION:
Sequence=AAH05567.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB012725; BAA31522.1; -; mRNA.
EMBL; AK017693; BAB30878.1; -; mRNA.
EMBL; AK032801; BAC28029.1; -; mRNA.
EMBL; AK146438; BAE27172.1; -; mRNA.
EMBL; AK162729; BAE37040.1; -; mRNA.
EMBL; BC037055; AAH37055.1; -; mRNA.
EMBL; BC005567; AAH05567.1; ALT_SEQ; mRNA.
CCDS; CCDS19496.1; -. [O88291-1]
RefSeq; NP_061229.2; NM_018759.2.
UniGene; Mm.248876; -.
ProteinModelPortal; O88291; -.
BioGrid; 207624; 3.
DIP; DIP-58947N; -.
IntAct; O88291; 3.
MINT; MINT-4105453; -.
STRING; 10090.ENSMUSP00000031227; -.
iPTMnet; O88291; -.
PhosphoSitePlus; O88291; -.
EPD; O88291; -.
MaxQB; O88291; -.
PaxDb; O88291; -.
PeptideAtlas; O88291; -.
PRIDE; O88291; -.
GeneID; 54367; -.
KEGG; mmu:54367; -.
UCSC; uc008ylj.3; mouse. [O88291-1]
CTD; 54367; -.
MGI; MGI:1927246; Zfp326.
eggNOG; ENOG410IGVY; Eukaryota.
eggNOG; ENOG4111H5U; LUCA.
HOGENOM; HOG000234349; -.
HOVERGEN; HBG080752; -.
InParanoid; O88291; -.
KO; K13204; -.
PhylomeDB; O88291; -.
TreeFam; TF105407; -.
PRO; PR:O88291; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_ZFP326; -.
GO; GO:0044609; C:DBIRD complex; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016363; C:nuclear matrix; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0000993; F:RNA polymerase II core binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:MGI.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 4.10.1050.10; -; 1.
InterPro; IPR007071; AKAP95.
InterPro; IPR026939; At2g23090-like.
InterPro; IPR034736; ZF_C2H2_AKAP95.
PANTHER; PTHR12190; PTHR12190; 1.
Pfam; PF04988; AKAP95; 1.
PROSITE; PS51799; ZF_C2H2_AKAP95; 2.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Complete proteome;
DNA-binding; Isopeptide bond; Metal-binding; Methylation;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 580 DBIRD complex subunit ZNF326.
/FTId=PRO_0000075387.
ZN_FING 314 336 C2H2 AKAP95-type 1. {ECO:0000255|PROSITE-
ProRule:PRU01140}.
ZN_FING 407 430 C2H2 AKAP95-type 2. {ECO:0000255|PROSITE-
ProRule:PRU01140}.
REGION 1 124 Mediates transcriptional activation.
MOTIF 238 260 Bipartite nuclear localization signal.
COMPBIAS 27 211 Gly-rich.
COMPBIAS 484 564 Glu-rich.
MOD_RES 48 48 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 173 173 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 235 235 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 247 247 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q5BKZ1}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 140 140 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q5BKZ1}.
CROSSLNK 240 240 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q5BKZ1}.
CROSSLNK 247 247 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q5BKZ1}.
CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q5BKZ1}.
CROSSLNK 264 264 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q5BKZ1}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q5BKZ1}.
CROSSLNK 459 459 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q5BKZ1}.
CROSSLNK 467 467 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q5BKZ1}.
VAR_SEQ 1 206 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014957.
VAR_SEQ 35 67 DRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGG -> AFKD
IYLKILLLSASKGEQHLIFFFLNSYRAGS (in isoform
3). {ECO:0000303|PubMed:16141072}.
/FTId=VSP_014958.
VAR_SEQ 68 580 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_014959.
CONFLICT 55 55 Q -> R (in Ref. 2; BAE27172).
{ECO:0000305}.
CONFLICT 494 494 D -> G (in Ref. 2; BAB30878/BAE37040).
{ECO:0000305}.
SEQUENCE 580 AA; 65225 MW; EF9672513D0FFC70 CRC64;
MDFEDDYVHS TCRGAYQDFN GMDRDYGPGS YGGLDRDYGH GSYGGQRSMD SYLNQSYGMD
NHSGGGGGSR FGPYESYDSR SSLGGRDLYR SGYGFNEPEQ TRFGGSYGGR FESSYRNSLD
SFGGRNQGGS SWEAPYSRSK LRPGFMEDRG RENYSSYSSF SSPHMKPAPV GSRGRGTPAY
PESTFGSRSY DAFGGPSTGR GRGRGHMGDF GSFHRPGIIV DYQNKPANVT IATARGIKRK
MMQIFIKPGG AFIKKPKLAK PMDKMNLSKS PTKTDPKNEE EEKRRIEARR EKQRRRREKN
SEKYGDGYRM AFTCSFCKFR TFEEKDIELH LESSSHQETL DHIQKQTKFD KVVMEFLHEC
MVNKFKKASI RKQQTLNHPE AYKIIEKDIM EGVTADDHMM KVETVHCSAC SVYIPALHSS
VQLHLKSPDH SKGKQAYKEQ IKRESVLTAT SILNNPIVKA RYERFVKGEN PFEIQDHPQD
QQIEGDEEDE EKIDEPIEEE EEEEEEEEEE GEEAGSVEEE GDVEGEEGTA EAAAAGEADA
VGEAEGAGEA EEAEEEEEEE GTQEFAAQAC ATEQCEHRQM


Related products :

Catalog number Product name Quantity
EIAAB46826 FANCC-interacting protein,Fanconi anemia zinc finger protein,FAZF,Homo sapiens,Human,Testis zinc finger protein,TZFP,ZBTB32,Zinc finger and BTB domain-containing protein 32,Zinc finger protein 538,ZNF
EIAAB47355 Homo sapiens,Human,Neurotrophin receptor-interacting factor homolog,SP2114,Zf2,Zinc finger protein 274,Zinc finger protein HFB101,Zinc finger protein with KRAB and SCAN domains 19,Zinc finger protein
EIAAB47457 Early B-cell factor-associated zinc finger protein,Ebfaz,Kiaa0760,Mouse,Mus musculus,Nur12,Oaz,Olf1_EBF-associated zinc finger protein,Smad- and Olf-interacting zinc finger protein,Zfp423,Zinc finger
EIAAB47340 BMZF5,BMZF-5,Bone marrow zinc finger 5,HD-ZNF1,Hematopoietic cell-derived zinc finger protein 1,Homo sapiens,Human,Zinc finger protein 254,Zinc finger protein 539,Zinc finger protein 91-like,ZNF254,ZN
EIAAB47388 Mouse,Mus musculus,Zan75,Zfp326,Zinc finger protein 326,Zinc finger protein-associated with nuclear matrix of 75 kDa,Znf326
EIAAB47314 BMZF2,BMZF-2,Bone marrow zinc finger 2,Homo sapiens,Human,KOX22,Zinc finger protein 224,Zinc finger protein 233,Zinc finger protein 255,Zinc finger protein 27,Zinc finger protein KOX22,ZNF224,ZNF233,Z
EIAAB46812 Homo sapiens,Human,MIZ1,Miz-1,Myc-interacting zinc finger protein 1,ZBTB17,Zinc finger and BTB domain-containing protein 17,Zinc finger protein 151,Zinc finger protein 60,ZNF151,ZNF60
EIAAB47352 CT-ZFP48,EBV-induced zinc finger protein,Epstein-Barr virus-induced zinc finger protein,Homo sapiens,Human,Zinc finger protein 271,Zinc finger protein dp,Zinc finger protein HZF7,Zinc finger protein Z
EIAAB47194 Homo sapiens,Human,Zf47,ZFP47,Zfp-47,Zinc finger and SCAN domain-containing protein 13,Zinc finger protein 306,Zinc finger protein 309,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and
EIAAB07456 CDKN1A-interacting zinc finger protein 1,Cip1-interacting zinc finger protein,CIZ1,Homo sapiens,Human,LSFR1,NP94,Nuclear protein NP94,Zinc finger protein 356,ZNF356
EIAAB47193 Mouse,Mus musculus,SCAN-KRAB-zinc finger protein,Skz1,Zf47,Zfp306,Zfp307,Zfp47,Zfp-47,Zinc finger protein 306,Zinc finger protein 307,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and S
EIAAB47395 C2H2-like zinc finger protein rearranged in thyroid adenomas,Homo sapiens,Human,RITA,Zinc finger protein 331,Zinc finger protein 361,Zinc finger protein 463,ZNF331,ZNF361,ZNF463
EIAAB47224 Homo sapiens,Human,MCH-R1-interacting zinc finger protein,Melanin-concentrating hormone receptor 1-interacting zinc finger protein,MIZIP,Zinc finger MYND domain-containing protein 19,ZMYND19
EIAAB47225 MCH-R1-interacting zinc finger protein,Melanin-concentrating hormone receptor 1-interacting zinc finger protein,Mizip,Mouse,Mus musculus,Zinc finger MYND domain-containing protein 19,Zmynd19
EIAAB47226 MCH-R1-interacting zinc finger protein,Melanin-concentrating hormone receptor 1-interacting zinc finger protein,Mizip,Rat,Rattus norvegicus,Zinc finger MYND domain-containing protein 19,Zmynd19
EIAAB14743 Fez family zinc finger protein 2,FEZF2,FEZL,FKSG36,Forebrain embryonic zinc finger-like protein 2,Homo sapiens,Human,Zinc finger protein 312,Zinc finger protein Fez-like,ZNF312
EIAAB47275 Homo sapiens,Human,Zinc finger protein 167,Zinc finger protein 448,Zinc finger protein 64,Zinc finger protein with KRAB and SCAN domains 7,ZKSCAN7,ZNF167,ZNF448,ZNF64
EIAAB47515 Mouse,Mus musculus,Nizp11,NSD1-interacting zinc finger protein 1,Zfp496,Zinc finger protein 496,Zinc finger protein with KRAB and SCAN domains 17,Zkscan17,Znf496
EIAAB47411 Homo sapiens,Human,KRAB zinc finger protein ZFQR,ZBRK1,Zinc finger and BRCA1-interacting protein with a KRAB domain 1,Zinc finger protein 350,Zinc finger protein ZBRK1,ZNF350
EIAAB47878 HDSG1,Heart development-specific gene 1 protein,Homo sapiens,Human,KOX11,Zinc finger protein 18,Zinc finger protein 535,Zinc finger protein KOX11,Zinc finger protein with KRAB and SCAN domains 6,ZKSCA
EIAAB47458 hOAZ,Homo sapiens,Human,KIAA0760,OAZ,Olf1_EBF-associated zinc finger protein,Smad- and Olf-interacting zinc finger protein,Zinc finger protein 423,ZNF423
EIAAB47384 Homo sapiens,Human,Zinc finger protein 322,Zinc finger protein 322A,Zinc finger protein 388,Zinc finger protein 489,ZNF322,ZNF322A,ZNF388,ZNF489
EIAAB14741 Fez,Fez family zinc finger protein 2,Fezf2,Fezl,Forebrain embryonic zinc finger-like protein 2,Mouse,Mus musculus,Zfp312,Zinc finger protein 312,Zinc finger protein Fez-like
EIAAB14742 Bos taurus,Bovine,Fez family zinc finger protein 2,FEZF2,FEZL,Forebrain embryonic zinc finger-like protein 2,Zinc finger protein 312,Zinc finger protein Fez-like,ZNF312
18-003-42276 Zinc finger and BTB domain-containing protein 7B - Zinc finger protein 67 homolog; Zfp-67; Zinc finger protein Th-POK; T-helper-inducing POZ_Krueppel-like factor; Krueppel-related zinc finger protein 0.1 mg Protein A


 

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