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LIM domain-binding protein 1 (LDB-1) (Carboxyl-terminal LIM domain-binding protein 2) (CLIM-2) (LIM domain-binding factor CLIM2) (mLdb1) (Nuclear LIM interactor)

 LDB1_MOUSE              Reviewed;         411 AA.
P70662; O55204; Q1EQX2; Q71V68;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
27-SEP-2017, entry version 149.
RecName: Full=LIM domain-binding protein 1;
Short=LDB-1;
AltName: Full=Carboxyl-terminal LIM domain-binding protein 2;
Short=CLIM-2;
AltName: Full=LIM domain-binding factor CLIM2;
Short=mLdb1;
AltName: Full=Nuclear LIM interactor;
Name=Ldb1; Synonyms=Nli;
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 3), FUNCTION, INTERACTION WITH
LHX1, AND TISSUE SPECIFICITY.
STRAIN=Swiss Webster; TISSUE=Embryo;
PubMed=8918878; DOI=10.1038/384270a0;
Agulnick A.D., Taira M., Breen J.J., Tanaka T., Dawid I.B.,
Westphal H.;
"Interactions of the LIM-domain-binding factor Ldb1 with LIM
homeodomain proteins.";
Nature 384:270-272(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Embryo;
PubMed=8876198; DOI=10.1073/pnas.93.21.11693;
Jurata L.W., Kenny D.A., Gill G.N.;
"Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting
protein, is expressed early in neuronal development.";
Proc. Natl. Acad. Sci. U.S.A. 93:11693-11698(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Embryonic head;
PubMed=9192866; DOI=10.1101/gad.11.11.1370;
Bach I., Carriere C., Ostendorff H.P., Andersen B., Rosenfeld M.G.;
"A family of LIM domain-associated cofactors confer transcriptional
synergism between LIM and Otx homeodomain proteins.";
Genes Dev. 11:1370-1380(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, INTERACTION WITH LMO2, AND
IDENTIFICATION IN A COMPLEX WITH LMO2 AND TAL1.
TISSUE=Yolk sac;
PubMed=9391090; DOI=10.1073/pnas.94.25.13707;
Visvader J.E., Mao X., Fujiwara Y., Hahm K., Orkin S.H.;
"The LIM-domain binding protein Ldb1 and its partner LMO2 act as
negative regulators of erythroid differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 94:13707-13712(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=9503020; DOI=10.1006/geno.1997.5163;
Yamashita T., Agulnick A.D., Copeland N.G., Gilbert D.J.,
Jenkins N.A., Westphal H.;
"Genomic structure and chromosomal localization of the mouse LIM
domain-binding protein 1 gene, Ldb1.";
Genomics 48:87-92(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE
SPLICING, AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=16815859; DOI=10.1093/jb/mvj134;
Tran Y.H., Xu Z., Kato A., Mistry A.C., Goya Y., Taira M.,
Brandt S.J., Hirose S.;
"Spliced isoforms of LIM-domain-binding protein (CLIM/NLI/Ldb) lacking
the LIM-interaction domain.";
J. Biochem. 140:105-119(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=FVB/N; TISSUE=Mammary gland;
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, INTERACTION WITH ISL1; LMO2 AND LMX1A, HOMODIMERIZATION,
SUBCELLULAR LOCATION, AND IDENTIFICATION OF LIM-BINDING DOMAIN.
PubMed=9315627; DOI=10.1128/MCB.17.10.5688;
Jurata L.W., Gill G.N.;
"Functional analysis of the nuclear LIM domain interactor NLI.";
Mol. Cell. Biol. 17:5688-5698(1997).
[9]
INTERACTION WITH LHX1, DOMAIN, AND HOMODIMERIZATION.
PubMed=9468533; DOI=10.1074/jbc.273.8.4712;
Breen J.J., Agulnick A.D., Westphal H., Dawid I.B.;
"Interactions between LIM domains and the LIM domain-binding protein
Ldb1.";
J. Biol. Chem. 273:4712-4717(1998).
[10]
INTERACTION WITH LHX6.
TISSUE=Fetal brain;
PubMed=10393337; DOI=10.1093/oxfordjournals.jbchem.a022420;
Kimura N., Ueno M., Nakashima K., Taga T.;
"A brain region-specific gene product Lhx6.1 interacts with Ldb1
through tandem LIM-domains.";
J. Biochem. 126:180-187(1999).
[11]
INTERACTION WITH LHX9.
PubMed=10330499; DOI=10.1016/S0925-4773(98)00233-0;
Bertuzzi S., Porter F.D., Pitts A., Kumar M., Agulnick A., Wassif C.,
Westphal H.;
"Characterization of Lhx9, a novel LIM/homeobox gene expressed by the
pioneer neurons in the mouse cerebral cortex.";
Mech. Dev. 81:193-198(1999).
[12]
FUNCTION, AND INTERACTION WITH LHX3 AND ISL1.
PubMed=12150931; DOI=10.1016/S0092-8674(02)00823-1;
Thaler J.P., Lee S.K., Jurata L.W., Gill G.N., Pfaff S.L.;
"LIM factor Lhx3 contributes to the specification of motor neuron and
interneuron identity through cell-type-specific protein-protein
interactions.";
Cell 110:237-249(2002).
[13]
INTERACTION WITH RLIM, AND UBIQUITINATION.
PubMed=11882901; DOI=10.1038/416099a;
Ostendorff H.P., Peirano R.I., Peters M.A., Schluter A., Bossenz M.,
Scheffner M., Bach I.;
"Ubiquitination-dependent cofactor exchange on LIM homeodomain
transcription factors.";
Nature 416:99-103(2002).
[14]
IDENTIFICATION IN A NUCLEAR TAL-1 COMPLEX.
PubMed=16407974; DOI=10.1038/sj.emboj.7600934;
Goardon N., Lambert J.A., Rodriguez P., Nissaire P., Herblot S.,
Thibault P., Dumenil D., Strouboulis J., Romeo P.-H., Hoang T.;
"ETO2 coordinates cellular proliferation and differentiation during
erythropoiesis.";
EMBO J. 25:357-366(2006).
[15]
INTERACTION WITH SLK, AND SUBCELLULAR LOCATION.
PubMed=19675209; DOI=10.1091/mbc.E08-07-0707;
Storbeck C.J., Wagner S., O'Reilly P., McKay M., Parks R.J.,
Westphal H., Sabourin L.A.;
"The Ldb1 and Ldb2 transcriptional cofactors interact with the Ste20-
like kinase SLK and regulate cell migration.";
Mol. Biol. Cell 20:4174-4182(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61 AND SER-302, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
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).
[17]
STRUCTURE BY NMR OF 336-375 IN COMPLEXES WITH LMO2 AND LMO4.
PubMed=12727888; DOI=10.1093/emboj/cdg196;
Deane J.E., Mackay J.P., Kwan A.H.Y., Sum E.Y.M., Visvader J.E.,
Matthews J.M.;
"Structural basis for the recognition of ldb1 by the N-terminal LIM
domains of LMO2 and LMO4.";
EMBO J. 22:2224-2233(2003).
[18]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 336-375 IN COMPLEX WITH LMO4.
PubMed=15343268; DOI=10.1038/sj.emboj.7600376;
Deane J.E., Ryan D.P., Sunde M., Maher M.J., Guss J.M., Visvader J.E.,
Matthews J.M.;
"Tandem LIM domains provide synergistic binding in the LMO4:Ldb1
complex.";
EMBO J. 23:3589-3598(2004).
-!- FUNCTION: Binds to the LIM domain of a wide variety of LIM domain-
containing transcription factors. May regulate the transcriptional
activity of LIM-containing proteins by determining specific
partner interactions. Plays a role in the development of
interneurons and motor neurons in cooperation with LHX3 and ISL1.
Acts synergistically with LHX1/LIM1 in axis formation and
activation of gene expression. Acts with LMO2 in the regulation of
red blood cell development, maintaining erythroid precursors in an
immature state. {ECO:0000269|PubMed:12150931,
ECO:0000269|PubMed:16815859, ECO:0000269|PubMed:8876198,
ECO:0000269|PubMed:8918878, ECO:0000269|PubMed:9192866,
ECO:0000269|PubMed:9315627, ECO:0000269|PubMed:9391090}.
-!- SUBUNIT: Interacts with ESR1 (By similarity). Forms homodimers and
heterodimers. Interacts with and activates LHX1/LIM1. Interacts
with the LIM domains of ISL1 and LMO2. Can assemble in a complex
with LMO2 and TAL1/SCL but does not interact with TAL1/SCL
directly. Strongly interacts with the LIM2 domain of LMX1A and
more weakly with the LIM1 domain. Homodimerization is not required
for, and does not effect, LMX1A-binding. Component of a nuclear
TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3.
Interacts with LHX6 and LHX9. At neuronal promoters, forms a
complex with LHX3 involved in the specification of interneurons,
in motor neurons, it is displaced by ISL1 to form a ternary
complex in which ISL1 contacts both LHX3 and LDB1. Interacts with
SLK; leading to negatively regulate SLK kinase activity
(PubMed:19675209). {ECO:0000250, ECO:0000269|PubMed:10330499,
ECO:0000269|PubMed:10393337, ECO:0000269|PubMed:11882901,
ECO:0000269|PubMed:12150931, ECO:0000269|PubMed:15343268,
ECO:0000269|PubMed:16407974, ECO:0000269|PubMed:19675209,
ECO:0000269|PubMed:8918878, ECO:0000269|PubMed:9315627,
ECO:0000269|PubMed:9391090, ECO:0000269|PubMed:9468533}.
-!- INTERACTION:
O54972:Cbfa2t3; NbExp=2; IntAct=EBI-6272082, EBI-8006703;
P61372:Isl1; NbExp=3; IntAct=EBI-6272082, EBI-7988215;
P50481:Lhx3; NbExp=5; IntAct=EBI-6272082, EBI-7988290;
P22091:Tal1; NbExp=4; IntAct=EBI-6272082, EBI-8006437;
Q60722:Tcf4; NbExp=2; IntAct=EBI-6272082, EBI-310070;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8876198,
ECO:0000269|PubMed:9315627, ECO:0000269|PubMed:9391090}.
Note=Colocalizes with SLK at leading edges (PubMed:19675209).
{ECO:0000269|PubMed:19675209}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Visvader-a;
IsoId=P70662-1; Sequence=Displayed;
Name=2; Synonyms=Tran-b;
IsoId=P70662-2; Sequence=VSP_027833, VSP_027834, VSP_027835;
Note=Due to intron retention. Lacks LIM-binding domain. Lacks
ability to activate LIM domain-dependent transcription.;
Name=3; Synonyms=Tran-a;
IsoId=P70662-3; Sequence=VSP_027833;
-!- TISSUE SPECIFICITY: Expression overlaps that of LIM domain-
containing proteins. Expressed widely in the embryo with highest
expression in several regions of the brain the central nervous
system ganglia. Also expressed in fetal liver, lung, kidney,
thymus and olfactory epithelium. Expressed in multiple adult
tissues including heart, brain, liver, kidney, testis, lung and
muscle and a diverse range of neuronal cell types, with expression
highest in the pituitary gland and skin. Expressed in both
embryonic and adult hemopoietic cells, including the erythroid
lineage. {ECO:0000269|PubMed:16815859, ECO:0000269|PubMed:8918878,
ECO:0000269|PubMed:9192866, ECO:0000269|PubMed:9391090}.
-!- DOMAIN: The dimerization domain is located in the N-terminus.
{ECO:0000269|PubMed:9468533}.
-!- PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by
the proteasome. {ECO:0000269|PubMed:11882901}.
-!- SIMILARITY: Belongs to the LDB family. {ECO:0000305}.
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EMBL; U70375; AAC52933.1; -; mRNA.
EMBL; U69270; AAC52887.1; -; mRNA.
EMBL; U89488; AAB96885.1; -; mRNA.
EMBL; AF030333; AAB94131.1; -; mRNA.
EMBL; AF024524; AAC40064.1; -; Genomic_DNA.
EMBL; AB250383; BAE95401.1; -; mRNA.
EMBL; BC013624; AAH13624.1; -; mRNA.
CCDS; CCDS29870.1; -. [P70662-3]
CCDS; CCDS50455.1; -. [P70662-1]
RefSeq; NP_001106879.1; NM_001113408.1. [P70662-1]
RefSeq; NP_034827.1; NM_010697.1. [P70662-3]
RefSeq; XP_011245459.1; XM_011247157.1. [P70662-3]
UniGene; Mm.327442; -.
PDB; 1J2O; NMR; -; A=336-375.
PDB; 1M3V; NMR; -; A=336-375.
PDB; 1RUT; X-ray; 1.30 A; X=336-375.
PDB; 2JTN; NMR; -; A=331-375.
PDB; 2L6Y; NMR; -; B=336-348.
PDB; 2L6Z; NMR; -; C=336-348.
PDB; 2LXD; NMR; -; A=336-375.
PDB; 4JCJ; X-ray; 3.00 A; A/B/C=336-366.
PDBsum; 1J2O; -.
PDBsum; 1M3V; -.
PDBsum; 1RUT; -.
PDBsum; 2JTN; -.
PDBsum; 2L6Y; -.
PDBsum; 2L6Z; -.
PDBsum; 2LXD; -.
PDBsum; 4JCJ; -.
ProteinModelPortal; P70662; -.
SMR; P70662; -.
BioGrid; 201125; 28.
CORUM; P70662; -.
DIP; DIP-42842N; -.
IntAct; P70662; 6.
MINT; MINT-2779250; -.
STRING; 10090.ENSMUSP00000118546; -.
iPTMnet; P70662; -.
PhosphoSitePlus; P70662; -.
MaxQB; P70662; -.
PaxDb; P70662; -.
PRIDE; P70662; -.
DNASU; 16825; -.
Ensembl; ENSMUST00000026252; ENSMUSP00000026252; ENSMUSG00000025223. [P70662-3]
Ensembl; ENSMUST00000056931; ENSMUSP00000053680; ENSMUSG00000025223. [P70662-3]
Ensembl; ENSMUST00000137771; ENSMUSP00000114667; ENSMUSG00000025223. [P70662-2]
Ensembl; ENSMUST00000156585; ENSMUSP00000118546; ENSMUSG00000025223. [P70662-1]
Ensembl; ENSMUST00000185355; ENSMUSP00000139562; ENSMUSG00000025223. [P70662-1]
GeneID; 16825; -.
KEGG; mmu:16825; -.
UCSC; uc008hrz.1; mouse. [P70662-1]
UCSC; uc008hsa.1; mouse. [P70662-2]
CTD; 8861; -.
MGI; MGI:894762; Ldb1.
eggNOG; KOG2181; Eukaryota.
eggNOG; ENOG410YZVH; LUCA.
GeneTree; ENSGT00390000005639; -.
HOGENOM; HOG000030908; -.
HOVERGEN; HBG000135; -.
InParanoid; P70662; -.
KO; K15617; -.
OMA; KMSVGCA; -.
OrthoDB; EOG091G0A0P; -.
PhylomeDB; P70662; -.
TreeFam; TF319923; -.
Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
ChiTaRS; Ldb1; mouse.
EvolutionaryTrace; P70662; -.
PRO; PR:P70662; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000025223; -.
CleanEx; MM_LDB1; -.
ExpressionAtlas; P70662; baseline and differential.
Genevisible; P70662; MM.
GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0001158; F:enhancer sequence-specific DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030274; F:LIM domain binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0043621; F:protein self-association; IPI:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0000989; F:transcription factor activity, transcription factor binding; IPI:MGI.
GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
GO; GO:0022607; P:cellular component assembly; IGI:MGI.
GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
GO; GO:0021549; P:cerebellum development; IMP:MGI.
GO; GO:0010669; P:epithelial structure maintenance; IGI:MGI.
GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
GO; GO:0001942; P:hair follicle development; IGI:MGI.
GO; GO:0060322; P:head development; IGI:UniProtKB.
GO; GO:0043973; P:histone H3-K4 acetylation; IMP:BHF-UCL.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0030182; P:neuron differentiation; IEP:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IGI:MGI.
GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0060319; P:primitive erythrocyte differentiation; TAS:BHF-UCL.
GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IMP:BHF-UCL.
GO; GO:0051893; P:regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0043549; P:regulation of kinase activity; IDA:UniProtKB.
GO; GO:0035019; P:somatic stem cell population maintenance; IGI:MGI.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:BHF-UCL.
GO; GO:0016055; P:Wnt signaling pathway; IMP:MGI.
InterPro; IPR030167; LDB1.
InterPro; IPR029005; LIM-bd/SEUSS.
PANTHER; PTHR10378; PTHR10378; 1.
PANTHER; PTHR10378:SF14; PTHR10378:SF14; 1.
Pfam; PF01803; LIM_bind; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Developmental protein; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q86U70}.
CHAIN 2 411 LIM domain-binding protein 1.
/FTId=PRO_0000084385.
REGION 336 374 LIM-binding domain (LID).
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q86U70}.
MOD_RES 61 61 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U70}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 36 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16815859,
ECO:0000303|PubMed:8876198,
ECO:0000303|PubMed:8918878,
ECO:0000303|PubMed:9192866}.
/FTId=VSP_027833.
VAR_SEQ 336 355 DVMVVGEPTLMGGEFGDEDE -> VSISAFFSSGLPHCSPL
TPV (in isoform 2).
{ECO:0000303|PubMed:16815859}.
/FTId=VSP_027834.
VAR_SEQ 356 411 Missing (in isoform 2).
{ECO:0000303|PubMed:16815859}.
/FTId=VSP_027835.
CONFLICT 262 262 Y -> C (in Ref. 3; AAB96885).
{ECO:0000305}.
CONFLICT 334 334 V -> A (in Ref. 3; AAB96885).
{ECO:0000305}.
CONFLICT 389 390 PW -> QR (in Ref. 3; AAB96885).
{ECO:0000305}.
STRAND 336 344 {ECO:0000244|PDB:1M3V}.
STRAND 346 349 {ECO:0000244|PDB:1J2O}.
STRAND 355 357 {ECO:0000244|PDB:1RUT}.
STRAND 359 362 {ECO:0000244|PDB:1RUT}.
SEQUENCE 411 AA; 46503 MW; 47C53DFA23044580 CRC64;
MSVGCACPGC SSKSFKLYSP KEPPNGNAFP PFHPGTMLDR DVGPTPMYPP TYLEPGIGRH
TPYGNQTDYR IFELNKRLQN WTEECDNLWW DAFTTEFFED DAMLTITFCL EDGPKRYTIG
RTLIPRYFRS IFEGGATELY YVLKHPKEAF HSNFVSLDCD QGSMVTQHGK PMFTQVCVEG
RLYLEFMFDD MMRIKTWHFS IRQHRELIPR SILAMHAQDP QMLDQLSKNI TRCGLSNSTL
NYLRLCVILE PMQELMSRHK TYSLSPRDCL KTCLFQKWQR MVAPPAEPAR QQPSKRRKRK
MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF GDEDERLITR
LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES KSENPTSQAS Q


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18-003-44214 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
18-003-43630 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
EIAAB46109 FBP21,FNBP21,Formin-binding protein 21,Homo sapiens,Human,WBP4,WBP-4,WW domain-binding protein 4,WW domain-containing-binding protein 4
EIAAB05064 Calcium-binding and coiled-coil domain-containing protein 2,Calcoco2,Mouse,Mus musculus,Ndp52,Ndp52l1,Nuclear domain 10 protein 52,Nuclear domain 10 protein NDP52
EIAAB46107 Fbp21,Fnbp21,Formin-binding protein 21,Mouse,Mus musculus,Wbp4,WBP-4,WW domain-binding protein 4,WW domain-containing-binding protein 4
EIAAB05062 Bos taurus,Bovine,Calcium-binding and coiled-coil domain-containing protein 2,CALCOCO2,NDP52,Nuclear domain 10 protein 52,Nuclear domain 10 protein NDP52
EIAAB27518 54 kDa nuclear RNA- and DNA-binding protein,55 kDa nuclear protein,DNA-binding p52_p100 complex, 52 kDa subunit,Homo sapiens,Human,NMT55,NONO,NonO protein,Non-POU domain-containing octamer-binding pro
29-121 NR1I2 belongs to the nuclear receptor superfamily, members of which are transcription factors characterized by a ligand-binding domain and a DNA-binding domain. NR1I2 contains a zinc finger domain.NR1 0.1 mg
25-312 NR1I2 belongs to the nuclear receptor superfamily, members of which are transcription factors characterized by a ligand-binding domain and a DNA-binding domain. NR1I2 contains a zinc finger domain.NR1 0.05 mg
29-080 NR1I2 belongs to the nuclear receptor superfamily, members of which are transcription factors characterized by a ligand-binding domain and a DNA-binding domain. NR1I2 contains a zinc finger domain.NR1 0.1 mg
EIAAB32306 GATA-3-binding protein G3B,Homo sapiens,Human,KMT8,Lysine N-methyltransferase 8,MTB-ZF,MTE-binding protein,PR domain zinc finger protein 2,PR domain-containing protein 2,PRDM2,Retinoblastoma protein-i
EIAAB46106 Formin-binding protein 21,Rat,Rattus norvegicus,Wbp4,WBP-4,WW domain-binding protein 4,WW domain-containing-binding protein 4
EIAAB32305 B lymphocyte-induced maturation protein 1,Beta-interferon gene positive regulatory domain I-binding factor,Blimp1,Blimp-1,Mouse,Mus musculus,PR domain zinc finger protein 1,PR domain-containing protei
EIAAB38239 Homo sapiens,Human,P1725,SH3 domain-binding glutamic acid-rich-like protein 3,SH3 domain-binding protein 1,SH3BGRL3,SH3BP-1
EIAAB38236 FASH3,Fovea-associated SH3 domain-binding protein,Homo sapiens,Human,SH3 domain-binding glutamic acid-rich-like protein 2,SH3BGRL2
EIAAB46103 Homo sapiens,Human,PAWP,Postacrosomal sheath WW domain-binding protein,WBP2NL,WW domain-binding protein 2-like
EIAAB12809 ELMO domain-containing protein 3,ELMOD3,Homo sapiens,Human,PP4068,RBED1,RBM29,RNA-binding motif and ELMO domain-containing protein 1,RNA-binding motif protein 29,RNA-binding protein 29
E1643h ELISA kit Brain-4,Brain-specific homeobox_POU domain protein 4,BRN4,Brn-4,Homo sapiens,Human,Oct-9,Octamer-binding protein 9,Octamer-binding transcription factor 9,OTF9,OTF-9,POU domain, class 3, tra 96T


 

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