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CCAAT/enhancer-binding protein beta (C/EBP beta) (AGP/EBP) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched transcriptional activator) (LAP)

 CEBPB_MOUSE             Reviewed;         296 AA.
P28033;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
25-OCT-2017, entry version 167.
RecName: Full=CCAAT/enhancer-binding protein beta {ECO:0000312|MGI:MGI:88373};
Short=C/EBP beta;
AltName: Full=AGP/EBP;
AltName: Full=Interleukin-6-dependent-binding protein;
Short=IL-6DBP;
AltName: Full=Liver-enriched transcriptional activator;
Short=LAP;
Name=Cebpb {ECO:0000312|MGI:MGI:88373};
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].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=1701020; DOI=10.1128/MCB.10.12.6642;
Chang C.J., Chen T.T., Lei H.Y., Chen D.S., Lee S.C.;
"Molecular cloning of a transcription factor, AGP/EBP, that belongs to
members of the C/EBP family.";
Mol. Cell. Biol. 10:6642-6653(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1840554; DOI=10.1101/gad.5.9.1538;
Cao Z., Umek R.M., McKnight S.L.;
"Regulated expression of three C/EBP isoforms during adipose
conversion of 3T3-L1 cells.";
Genes Dev. 5:1538-1552(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
TISSUE=Liver;
PubMed=7598808; DOI=10.1089/dna.1995.14.529;
Chang C.J., Shen B.J., Lee S.C.;
"Autoregulated induction of the acute-phase response transcription
factor gene, agp/ebp.";
DNA Cell Biol. 14:529-537(1995).
[4]
FUNCTION, PHOSPHORYLATION AT SER-276, AND MUTAGENESIS OF SER-276.
PubMed=1314426; DOI=10.1126/science.256.5055.370;
Wegner M., Cao Z., Rosenfeld M.G.;
"Calcium-regulated phosphorylation within the leucine zipper of C/EBP
beta.";
Science 256:370-373(1992).
[5]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=9303532; DOI=10.1101/gad.11.17.2153;
Sterneck E., Tessarollo L., Johnson P.F.;
"An essential role for C/EBPbeta in female reproduction.";
Genes Dev. 11:2153-2162(1997).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9727068; DOI=10.1172/JCI3135;
Greenbaum L.E., Li W., Cressman D.E., Peng Y., Ciliberto G., Poli V.,
Taub R.;
"CCAAT enhancer- binding protein beta is required for normal
hepatocyte proliferation in mice after partial hepatectomy.";
J. Clin. Invest. 102:996-1007(1998).
[7]
INTERACTION WITH TRIM28.
PubMed=9742105; DOI=10.1128/MCB.18.10.5880;
Chang C.J., Chen Y.L., Lee S.C.;
"Coactivator TIF1beta interacts with transcription factor C/EBPbeta
and glucocorticoid receptor to induce alpha1-acid glycoprotein gene
expression.";
Mol. Cell. Biol. 18:5880-5887(1998).
[8]
FUNCTION, PHOSPHORYLATION AT THR-217, AND MUTAGENESIS OF THR-217.
PubMed=10635333; DOI=10.1016/S1097-2765(00)80237-3;
Buck M., Poli V., van der Geer P., Chojkier M., Hunter T.;
"Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP
beta is required for hepatocyte proliferation induced by TGF alpha.";
Mol. Cell 4:1087-1092(1999).
[9]
INTERACTION WITH MYB.
PubMed=11792321; DOI=10.1016/S0092-8674(01)00636-5;
Tahirov T.H., Sato K., Ichikawa-Iwata E., Sasaki M., Inoue-Bungo T.,
Shiina M., Kimura K., Takata S., Fujikawa A., Morii H., Kumasaka T.,
Yamamoto M., Ishii S., Ogata K.;
"Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a
promoter.";
Cell 108:57-70(2002).
[10]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=15509779; DOI=10.1128/MCB.24.22.9744-9751.2004;
Begay V., Smink J., Leutz A.;
"Essential requirement of CCAAT/enhancer binding proteins in
embryogenesis.";
Mol. Cell. Biol. 24:9744-9751(2004).
[11]
INTERACTION WITH CCDC85B.
PubMed=15644333; DOI=10.1074/jbc.M411741200;
Bezy O., Elabd C., Cochet O., Petersen R.K., Kristiansen K., Dani C.,
Ailhaud G., Amri E.-Z.;
"Delta-interacting protein A, a new inhibitory partner of
CCAAT/enhancer-binding protein beta, implicated in adipocyte
differentiation.";
J. Biol. Chem. 280:11432-11438(2005).
[12]
INTERACTION WITH PTGES2.
PubMed=15879117; DOI=10.4049/jimmunol.174.10.6203;
Meng Q., Raha A., Roy S., Hu J., Kalvakolanu D.V.;
"IFN-gamma-stimulated transcriptional activation by IFN-gamma-
activated transcriptional element-binding factor 1 occurs via an
inducible interaction with CAAAT/enhancer-binding protein-beta.";
J. Immunol. 174:6203-6211(2005).
[13]
FUNCTION, PHOSPHORYLATION AT THR-179; SER-184 AND THR-188,
DNA-BINDING, MUTAGENESIS OF THR-179; SER-184 AND THR-188,
IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=15985551; DOI=10.1073/pnas.0503891102;
Tang Q.Q., Gronborg M., Huang H., Kim J.W., Otto T.C., Pandey A.,
Lane M.D.;
"Sequential phosphorylation of CCAAT enhancer-binding protein beta by
MAPK and glycogen synthase kinase 3beta is required for
adipogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 102:9766-9771(2005).
[14]
FUNCTION, SUMOYLATION AT LYS-133, TISSUE SPECIFICITY, MUTAGENESIS OF
LYS-133, AND SUBCELLULAR LOCATION.
PubMed=16585579; DOI=10.4049/jimmunol.176.8.4843;
Berberich-Siebelt F., Berberich I., Andrulis M., Santner-Nanan B.,
Jha M.K., Klein-Hessling S., Schimpl A., Serfling E.;
"SUMOylation interferes with CCAAT/enhancer-binding protein beta-
mediated c-myc repression, but not IL-4 activation in T cells.";
J. Immunol. 176:4843-4851(2006).
[15]
FUNCTION, DISRUPTION PHENOTYPE, AND ALTERNATIVE INITIATION.
PubMed=17911624; DOI=10.4049/jimmunol.179.8.5378;
Uematsu S., Kaisho T., Tanaka T., Matsumoto M., Yamakami M., Omori H.,
Yamamoto M., Yoshimori T., Akira S.;
"The C/EBP beta isoform 34-kDa LAP is responsible for NF-IL-6-mediated
gene induction in activated macrophages, but is not essential for
intracellular bacteria killing.";
J. Immunol. 179:5378-5386(2007).
[16]
FUNCTION, ACETYLATION AT LYS-98; LYS-101 AND LYS-102, INTERACTION WITH
KAT2A AND KAT2B, AND MUTAGENESIS OF LYS-98; LYS-101 AND LYS-102.
PubMed=17301242; DOI=10.1073/pnas.0607378104;
Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.;
"Glucocorticoid-stimulated preadipocyte differentiation is mediated
through acetylation of C/EBPbeta by GCN5.";
Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007).
[17]
FUNCTION, PHOSPHORYLATION AT THR-179; SER-184 AND THR-188, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17601773; DOI=10.1073/pnas.0703771104;
Li X., Kim J.W., Gronborg M., Urlaub H., Lane M.D., Tang Q.Q.;
"Role of cdk2 in the sequential phosphorylation/activation of
C/EBPbeta during adipocyte differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 104:11597-11602(2007).
[18]
METHYLATION AT LYS-39.
PubMed=18647749; DOI=10.1074/jbc.M802132200;
Pless O., Kowenz-Leutz E., Knoblich M., Lausen J., Beyermann M.,
Walsh M.J., Leutz A.;
"G9a-mediated lysine methylation alters the function of
CCAAT/enhancer-binding protein-beta.";
J. Biol. Chem. 283:26357-26363(2008).
[19]
FUNCTION, INTERACTION WITH EP300, MUTAGENESIS OF LYS-39; LYS-98 AND
LYS-215, AND ACETYLATION AT LYS-39.
PubMed=18486321; DOI=10.1016/j.mce.2008.03.009;
Cesena T.I., Cui T.X., Subramanian L., Fulton C.T.,
Iniguez-Lluhi J.A., Kwok R.P., Schwartz J.;
"Acetylation and deacetylation regulate CCAAT/enhancer binding protein
beta at K39 in mediating gene transcription.";
Mol. Cell. Endocrinol. 289:94-101(2008).
[20]
SUBCELLULAR LOCATION, AND COMPLEX FORMATION WITH THOC5.
PubMed=19015024; DOI=10.1016/j.cellsig.2008.10.018;
Carney L., Pierce A., Rijnen M., Gonzalez Sanchez M.B., Hamzah H.G.,
Zhang L., Tamura T., Whetton A.D.;
"THOC5 couples M-CSF receptor signaling to transcription factor
expression.";
Cell. Signal. 21:309-316(2009).
[21]
FUNCTION (ISOFORM 1 AND ISOFORM 3), TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
PubMed=19440205; DOI=10.1038/emboj.2009.127;
Smink J.J., Begay V., Schoenmaker T., Sterneck E., de Vries T.J.,
Leutz A.;
"Transcription factor C/EBPbeta isoform ratio regulates
osteoclastogenesis through MafB.";
EMBO J. 28:1769-1781(2009).
[22]
FUNCTION, GLYCOSYLATION AT SER-180 AND SER-181, MUTAGENESIS OF SER-180
AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION
AT THR-179; SER-184 AND THR-188.
PubMed=19478079; DOI=10.1074/jbc.M109.005678;
Li X., Molina H., Huang H., Zhang Y.Y., Liu M., Qian S.W., Slawson C.,
Dias W.B., Pandey A., Hart G.W., Lane M.D., Tang Q.Q.;
"O-linked N-acetylglucosamine modification on CCAAT enhancer-binding
protein beta: role during adipocyte differentiation.";
J. Biol. Chem. 284:19248-19254(2009).
[23]
FUNCTION IN ADIPOGENESIS, INTERACTION WITH EP300 AND RORA, ALTERNATIVE
SPLICING (ISOFORMS 2 AND 3), AND PHOSPHORYLATION AT THR-188.
PubMed=19324970; DOI=10.1210/me.2008-0277;
Ohoka N., Kato S., Takahashi Y., Hayashi H., Sato R.;
"The orphan nuclear receptor RORalpha restrains adipocyte
differentiation through a reduction of C/EBPbeta activity and
perilipin gene expression.";
Mol. Endocrinol. 23:759-771(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, DISRUPTION PHENOTYPE,
INTERACTION WITH PRDM16, INDUCTION BY COLD EXPOSURE, AND TISSUE
SPECIFICITY.
PubMed=19641492; DOI=10.1038/nature08262;
Kajimura S., Seale P., Kubota K., Lunsford E., Frangioni J.V.,
Gygi S.P., Spiegelman B.M.;
"Initiation of myoblast to brown fat switch by a PRDM16-C/EBP-beta
transcriptional complex.";
Nature 460:1154-1158(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND THR-188, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, and Lung;
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).
[26]
FUNCTION, INTERACTION WITH MED23; MED26; SMARCA2; SMARCB1 AND SMARCC1,
IDENTIFICATION BY MASS SPECTROMETRY, AND METHYLATION AT ARG-3.
PubMed=20111005; DOI=10.1038/emboj.2010.3;
Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
"Crosstalk between C/EBPbeta phosphorylation, arginine methylation,
and SWI/SNF/Mediator implies an indexing transcription factor code.";
EMBO J. 29:1105-1115(2010).
[27]
FUNCTION, SUMOYLATION AT LYS-133, DESUMOYLATION AT LYS-133,
MUTAGENESIS OF LYS-133 AND GLU-135, AND UBIQUITINATION.
PubMed=20194620; DOI=10.1128/MCB.00852-09;
Chung S.S., Ahn B.Y., Kim M., Choi H.H., Park H.S., Kang S.,
Park S.G., Kim Y.B., Cho Y.M., Lee H.K., Chung C.H., Park K.S.;
"Control of adipogenesis by the SUMO-specific protease SENP2.";
Mol. Cell. Biol. 30:2135-2146(2010).
[28]
INTERACTION WITH ZNF638.
PubMed=21602272; DOI=10.1074/jbc.M110.212506;
Meruvu S., Hugendubler L., Mueller E.;
"Regulation of adipocyte differentiation by the zinc finger protein
ZNF638.";
J. Biol. Chem. 286:26516-26523(2011).
[29]
INTERACTION WITH CIDEA AND CIDEC.
PubMed=22245780; DOI=10.1038/nm.2614;
Wang W., Lv N., Zhang S., Shui G., Qian H., Zhang J., Chen Y., Ye J.,
Xie Y., Shen Y., Wenk M.R., Li P.;
"Cidea is an essential transcriptional coactivator regulating mammary
gland secretion of milk lipids.";
Nat. Med. 18:235-243(2012).
[30]
FUNCTION, SUMOYLATION AT LYS-133, MUTAGENESIS OF LYS-133, AND
UBIQUITINATION.
PubMed=24061474; DOI=10.1128/MCB.00723-13;
Liu Y., Zhang Y.D., Guo L., Huang H.Y., Zhu H., Huang J.X., Liu Y.,
Zhou S.R., Dang Y.J., Li X., Tang Q.Q.;
"Protein inhibitor of activated STAT 1 (PIAS1) is identified as the
SUMO E3 ligase of CCAAT/enhancer-binding protein beta (C/EBPbeta)
during adipogenesis.";
Mol. Cell. Biol. 33:4606-4617(2013).
[31]
FUNCTION, AND INTERACTION WITH ATF5 AND EP300.
PubMed=24216764; DOI=10.1128/MCB.00956-13;
Zhao Y., Zhang Y.D., Zhang Y.Y., Qian S.W., Zhang Z.C., Li S.F.,
Guo L., Liu Y., Wen B., Lei Q.Y., Tang Q.Q., Li X.;
"p300-dependent acetylation of activating transcription factor 5
enhances C/EBPbeta transactivation of C/EBPalpha during 3T3-L1
differentiation.";
Mol. Cell. Biol. 34:315-324(2014).
[32]
REVIEW OF PTMS AND FUNCTION.
PubMed=25451943; DOI=10.1074/jbc.R114.619957;
Guo L., Li X., Tang Q.;
"Transcriptional Regulation of Adipocyte Differentiation: A Central
Role for CCAAT/Enhancer-binding Protein (C/EBP) beta.";
J. Biol. Chem. 290:755-761(2015).
[33]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 224-285 IN COMPLEX WITH
ATF4, INTERACTION WITH ATF4, AND DNA-BINDING.
PubMed=11018027; DOI=10.1074/jbc.M005594200;
Podust L.M., Krezel A.M., Kim Y.;
"Crystal structure of the CCAAT box/enhancer-binding protein beta
activating transcription factor-4 basic leucine zipper heterodimer in
the absence of DNA.";
J. Biol. Chem. 276:505-513(2001).
-!- FUNCTION: Important transcription factor regulating the expression
of genes involved in immune and inflammatory responses
(PubMed:16585579, PubMed:17911624, PubMed:18486321,
PubMed:20111005). Plays also a significant role in adipogenesis,
as well as in the gluconeogenic pathway, liver regeneration, and
hematopoiesis (PubMed:9727068, PubMed:10635333, PubMed:17301242,
PubMed:17601773, PubMed:19478079, PubMed:24061474,
PubMed:24216764). The consensus recognition site is 5'-
T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein
interactions and post-translational protein modifications. During
early embryogenesis, plays essential and redundant functions with
CEBPA (PubMed:15509779). Has a promitotic effect on many cell
types such as hepatocytes and adipocytes but has an
antiproliferative effect on T-cells by repressing MYC expression,
facilitating differentiation along the T-helper 2 lineage
(PubMed:9727068, PubMed:10635333, PubMed:16585579). Binds to
regulatory regions of several acute-phase and cytokines genes and
plays a role in the regulation of acute-phase reaction and
inflammation. Plays also a role in intracellular bacteria killing
(PubMed:17911624). During adipogenesis, is rapidly expressed and,
after activation by phosphorylation, induces CEBPA and PPARG,
which turn on the series of adipocyte genes that give rise to the
adipocyte phenotype. The delayed transactivation of the CEBPA and
PPARG genes by CEBPB appears necessary to allow mitotic clonal
expansion and thereby progression of terminal differentiation
(PubMed:15985551, PubMed:17301242, PubMed:17601773,
PubMed:20194620). Essential for female reproduction because of a
critical role in ovarian follicle development (PubMed:9303532).
Restricts osteoclastogenesis (PubMed:19440205).
{ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:10635333,
ECO:0000269|PubMed:1314426, ECO:0000269|PubMed:15509779,
ECO:0000269|PubMed:15985551, ECO:0000269|PubMed:16585579,
ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:17601773,
ECO:0000269|PubMed:17911624, ECO:0000269|PubMed:18486321,
ECO:0000269|PubMed:19440205, ECO:0000269|PubMed:19478079,
ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:20194620,
ECO:0000269|PubMed:24061474, ECO:0000269|PubMed:24216764,
ECO:0000269|PubMed:9303532, ECO:0000269|PubMed:9727068,
ECO:0000303|PubMed:25451943}.
-!- FUNCTION: Isoform 2: Essential for gene expression induction in
activated macrophages. Plays a major role in immune responses such
as CD4(+) T-cell response, granuloma formation and endotoxin
shock. Not essential for intracellular bacteria killing.
{ECO:0000269|PubMed:17911624}.
-!- FUNCTION: Isoform 3: Acts as a dominant negative through
heterodimerization with isoform 2 (By similarity). Promotes
osteoblast differentiation and osteoclastogenesis
(PubMed:19440205). {ECO:0000250|UniProtKB:P17676,
ECO:0000250|UniProtKB:P21272, ECO:0000269|PubMed:19440205}.
-!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Interacts
with ATF4. Binds DNA as a heterodimer with ATF4 (PubMed:11018027).
Interacts with MYB; within the complex, MYB and CEBPB bind to
different promoter regions (PubMed:11792321). Can form stable
heterodimers with CEBPA, CEBPD and CEBPE (By similarity). Isoform
2 and isoform 3 also form heterodimers (By similarity). Interacts
with TRIM28 and PTGES2 (PubMed:9742105, PubMed:15879117).
Interacts with PRDM16 (PubMed:19641492). Interacts with CCDC85B
(PubMed:15644333). Forms a complex with THOC5 (PubMed:19015024).
Interacts with ZNF638; this interaction increases transcriptional
activation (PubMed:21602272). Interacts with CIDEA and CIDEC
(PubMed:22245780). Interaction with CIDEA increases
transcriptional activation of a subset of CEBPB downstream target
genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH. Interaction
with CIDEC increases transcriptional activation of SOCS1, SOCS3,
TGFB1, TGFBR1, ID2 and XDH. Interacts with DDIT3/CHOP. Interacts
with EP300; recruits EP300 to chromatin. Interacts with RORA; the
interaction disrupts interaction with EP300 (PubMed:19324970).
Interacts (not methylated) with MED23, MED26, SMARCA2, SMARCB1 and
SMARCC1 (PubMed:20111005). Interacts with KAT2A and KAT2B
(PubMed:17301242). Interacts with ATF5; EP300 is required for ATF5
and CEBPB interaction and DNA binding (PubMed:24216764).
{ECO:0000250|UniProtKB:P21272, ECO:0000269|PubMed:11018027,
ECO:0000269|PubMed:11792321, ECO:0000269|PubMed:15644333,
ECO:0000269|PubMed:15879117, ECO:0000269|PubMed:17301242,
ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:19015024,
ECO:0000269|PubMed:19324970, ECO:0000269|PubMed:19641492,
ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:21602272,
ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:24216764,
ECO:0000269|PubMed:9742105}.
-!- INTERACTION:
Q99PV5:Bhlhe41; NbExp=5; IntAct=EBI-1029979, EBI-6143801;
Q9JHD2:Kat2a; NbExp=5; IntAct=EBI-1029979, EBI-2943116;
Q92831:KAT2B (xeno); NbExp=2; IntAct=EBI-1029979, EBI-477430;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16585579,
ECO:0000269|PubMed:19015024}. Cytoplasm
{ECO:0000250|UniProtKB:P17676}. Note=In T-cells when sumoylated
drawn to pericentric heterochromatin thereby allowing
proliferation (PubMed:16585579). Translocates to the nucleus when
phosphorylated at Ser-288 (By similarity).
{ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:16585579}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=1; Synonyms=a, C/EBPbeta-FL, LAP*;
IsoId=P28033-1; Sequence=Displayed;
Name=2; Synonyms=b, C/EBPbeta-LAP;
IsoId=P28033-3; Sequence=VSP_053977;
Note=Major isoform.;
Name=3; Synonyms=c, C/EBPbeta-LIP;
IsoId=P28033-2; Sequence=VSP_053976;
-!- TISSUE SPECIFICITY: Abundantly expressed in myoblasts. Enriched in
brown adipose tissue (BAT) versus white adipose tissue (WAT).
Expressed in hepatocytes (at protein level). Expressed in T
lymphocytes (PubMed:16585579). The expression in granulosa cells
of antral follicles is induced by luteinizing hormone
(PubMed:9303532). Expressed in chondrocytes and osteoblasts (at
protein level) (PubMed:19440205). {ECO:0000269|PubMed:10635333,
ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:19440205,
ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:9303532}.
-!- DEVELOPMENTAL STAGE: At E9.5, expressed in the chorionic plate and
ectoplacental cone. From E10.5 to at least E11.5, is also
expressed in the trophoblast cells of the three placenta layers
(PubMed:15509779). Expressed in monocytic precursors but is
vanished during differentiation into osteoclasts. The expression
increases during osteoblast differentiation (PubMed:19440205).
{ECO:0000269|PubMed:15509779, ECO:0000269|PubMed:19440205}.
-!- INDUCTION: Up-regulated by cold exposure.
{ECO:0000269|PubMed:19641492}.
-!- PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3. Sumoylation
at Lys-133 is required for inhibition of T-cells proliferation
(PubMed:16585579). In adipocytes, sumoylation at Lys-133 by PIAS1
leads to ubiquitination and subsequent proteasomal degradation
(PubMed:24061474). Desumoylated by SENP2, which abolishes
ubiquitination and stabilizes protein levels (PubMed:20194620).
{ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:16585579,
ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:24061474}.
-!- PTM: Ubiquitinated, leading to proteasomal degradation.
{ECO:0000269|PubMed:24061474}.
-!- PTM: Phosphorylated at Thr-188 by MAPK and CDK2, serves to prime
phosphorylation at Thr-179 and Ser-184 by GSK3B and acquire DNA-
binding as well as transactivation activities, required to induce
adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-188
in the primed phosphorylated state during mitotical cloning
expansion and thereby progression of terminal differentiation.
Phosphorylation at Thr-217 enhances transactivation activity.
Phosphorylation at Ser-276 in response to calcium increases
transactivation activity (PubMed:1314426). Phosphorylated at Thr-
188 by RPS6KA1 (By similarity). {ECO:0000250|UniProtKB:P17676,
ECO:0000269|PubMed:1314426, ECO:0000269|PubMed:15985551,
ECO:0000269|PubMed:17601773}.
-!- PTM: O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents
phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding
activity which delays the adipocyte differentiation program.
{ECO:0000269|PubMed:19478079}.
-!- PTM: Acetylated. Acetylation at Lys-39 is an important and dynamic
regulatory event that contributes to its ability to transactivate
target genes, including those associated with adipogenesis and
adipocyte function. Deacetylation by HDAC1 represses its
transactivation activity (PubMed:18486321). Acetylated by KAT2A
and KAT2B within a cluster of lysine residues between amino acids
98-102, this acetylation is strongly induced by glucocorticoid
treatment and enhances transactivation activity (PubMed:17301242).
{ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:18486321}.
-!- PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by
EHMT2, inhibits transactivation activity. Methylation is probably
inhibited by phosphorylation at Thr-188.
{ECO:0000269|PubMed:20111005, ECO:0000305|PubMed:18647749}.
-!- DISRUPTION PHENOTYPE: Embryos display defects in brown fat tissue
development (PubMed:19641492). Females are sterile, ovaries lack
corpora lutea (PubMed:9303532). Upon bacterial infection, animals
show impaired bactericidal activity and die within 3 days
(PubMed:17911624). Posthepatectomy, animals show a reduced
regenerative response with DNA synthesis decreased to 25% of
normal in hepatocytes and a prolonged period of hypoglycemia
(PubMed:9727068). Animals show osteopenia with decreased bone
formation and enhanced ostecolastogensis. Long bones have a 1.6
fold diminished bone volume with a reduction of the number and
thickness of bone trabeculae (PubMed:19440205). Mutants of isoform
2 show impaired CSF3/G-CSF production by macrophages, IFNG
production by CD4(+) T-cells and granuloma formation in liver.
Upon bacterial infection, mutants of isoform 2 die within 6 days.
Resistant to LPS-induced endotoxin shock (PubMed:17911624). Double
knockout CEBPA and CEBPB results in embryonic developmental arrest
and death at around E10 to E11, associated with a gross placenta
failure (PubMed:15509779). {ECO:0000269|PubMed:15509779,
ECO:0000269|PubMed:17911624, ECO:0000269|PubMed:19440205,
ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:9303532,
ECO:0000269|PubMed:9727068}.
-!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M61007; AAA37192.1; -; mRNA.
EMBL; X62600; CAA44484.1; -; mRNA.
EMBL; S78572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS17105.1; -. [P28033-1]
PIR; A36366; A36366.
RefSeq; NP_001274667.1; NM_001287738.1. [P28033-3]
RefSeq; NP_001274668.1; NM_001287739.1. [P28033-2]
RefSeq; NP_034013.1; NM_009883.4. [P28033-1]
UniGene; Mm.439656; -.
PDB; 1CI6; X-ray; 2.60 A; B=224-285.
PDBsum; 1CI6; -.
ProteinModelPortal; P28033; -.
SMR; P28033; -.
BioGrid; 198669; 16.
DIP; DIP-37539N; -.
IntAct; P28033; 14.
STRING; 10090.ENSMUSP00000069850; -.
iPTMnet; P28033; -.
PhosphoSitePlus; P28033; -.
PaxDb; P28033; -.
PeptideAtlas; P28033; -.
PRIDE; P28033; -.
DNASU; 12608; -.
Ensembl; ENSMUST00000070642; ENSMUSP00000069850; ENSMUSG00000056501. [P28033-1]
GeneID; 12608; -.
KEGG; mmu:12608; -.
UCSC; uc008oaf.2; mouse. [P28033-1]
CTD; 1051; -.
MGI; MGI:88373; Cebpb.
eggNOG; KOG3119; Eukaryota.
eggNOG; ENOG410YJ8G; LUCA.
GeneTree; ENSGT00530000063192; -.
HOGENOM; HOG000013112; -.
HOVERGEN; HBG050879; -.
InParanoid; P28033; -.
KO; K10048; -.
OMA; CKKPAEY; -.
OrthoDB; EOG091G11FC; -.
PhylomeDB; P28033; -.
TreeFam; TF105008; -.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
ChiTaRS; Cebpb; mouse.
EvolutionaryTrace; P28033; -.
PRO; PR:P28033; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000056501; -.
CleanEx; MM_CEBPB; -.
ExpressionAtlas; P28033; baseline and differential.
Genevisible; P28033; MM.
GO; GO:0036488; C:CHOP-C/EBP complex; IEA:Ensembl.
GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0016363; C:nuclear matrix; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0035259; F:glucocorticoid receptor binding; IEA:Ensembl.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:MGI.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB.
GO; GO:0050873; P:brown fat cell differentiation; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0001892; P:embryonic placenta development; IGI:MGI.
GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
GO; GO:0002432; P:granuloma formation; IMP:UniProtKB.
GO; GO:0072574; P:hepatocyte proliferation; IDA:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
GO; GO:0097421; P:liver regeneration; IMP:UniProtKB.
GO; GO:0060644; P:mammary gland epithelial cell differentiation; IMP:MGI.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IMP:MGI.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0030182; P:neuron differentiation; IDA:MGI.
GO; GO:0001541; P:ovarian follicle development; IMP:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0045408; P:regulation of interleukin-6 biosynthetic process; IDA:MGI.
GO; GO:0045670; P:regulation of osteoclast differentiation; IDA:UniProtKB.
GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:BHF-UCL.
GO; GO:0035711; P:T-helper 1 cell activation; IMP:UniProtKB.
InterPro; IPR004827; bZIP.
InterPro; IPR016468; C/EBP_chordates.
Pfam; PF07716; bZIP_2; 1.
PIRSF; PIRSF005879; CCAAT/enhancer-binding; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative initiation;
Complete proteome; Cytoplasm; Differentiation; DNA-binding;
Glycoprotein; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 296 CCAAT/enhancer-binding protein beta.
/FTId=PRO_0000076618.
DOMAIN 222 285 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 22 Required for Lys-133 sumoylation.
{ECO:0000250|UniProtKB:P17676}.
REGION 22 104 Required for MYC transcriptional
repression.
{ECO:0000269|PubMed:16585579}.
REGION 226 246 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 248 255 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 120 129 Pro-rich.
COMPBIAS 170 191 Pro/Ser-rich.
MOD_RES 3 3 Omega-N-methylated arginine; by CARM1.
{ECO:0000269|PubMed:20111005}.
MOD_RES 39 39 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:18486321}.
MOD_RES 39 39 N6-methylated lysine; alternate.
{ECO:0000305|PubMed:18647749}.
MOD_RES 98 98 N6-acetyllysine; by KAT2A and KAT2B.
{ECO:0000305|PubMed:17301242}.
MOD_RES 101 101 N6-acetyllysine; by KAT2A and KAT2B.
{ECO:0000305|PubMed:17301242}.
MOD_RES 102 102 N6-acetyllysine; by KAT2A and KAT2B;
alternate. {ECO:0000305|PubMed:17301242}.
MOD_RES 179 179 Phosphothreonine; by GSK3-beta.
{ECO:0000269|PubMed:15985551,
ECO:0000269|PubMed:17601773,
ECO:0000269|PubMed:19478079}.
MOD_RES 184 184 Phosphoserine; by GSK3-beta.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15985551,
ECO:0000269|PubMed:17601773,
ECO:0000269|PubMed:19478079}.
MOD_RES 188 188 Phosphothreonine; by RPS6KA1, CDK2 and
MAPK. {ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15985551,
ECO:0000269|PubMed:17601773,
ECO:0000269|PubMed:19324970,
ECO:0000269|PubMed:19478079}.
MOD_RES 217 217 Phosphothreonine; by RPS6KA1 and
PKC/PRKCA. {ECO:0000269|PubMed:10635333}.
MOD_RES 239 239 Phosphoserine; by PKC/PRKCA.
{ECO:0000250|UniProtKB:P17676}.
MOD_RES 276 276 Phosphoserine; by CaMK2.
{ECO:0000305|PubMed:1314426}.
CARBOHYD 180 180 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:19478079}.
CARBOHYD 181 181 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:19478079}.
CROSSLNK 102 102 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P17676}.
CROSSLNK 133 133 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:16585579,
ECO:0000269|PubMed:20194620,
ECO:0000269|PubMed:24061474}.
CROSSLNK 133 133 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P17676}.
CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17676}.
CROSSLNK 211 211 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17676}.
CROSSLNK 213 213 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17676}.
CROSSLNK 283 283 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17676}.
VAR_SEQ 1 151 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_053976.
VAR_SEQ 1 21 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_053977.
MUTAGEN 39 39 K->A,Q: No effect on interaction with
EP300. {ECO:0000269|PubMed:18486321}.
MUTAGEN 39 39 K->R: Dominant negative. Loss of
transactivation activity. No effect on
interaction with EP300.
{ECO:0000269|PubMed:18486321}.
MUTAGEN 98 98 K->R: No effect on transactivation
activity. Not acetylated after
glucocorticoid-stimulation and no
increase of transactivation activity;
when associated with R-101 and R-102.
{ECO:0000269|PubMed:17301242,
ECO:0000269|PubMed:18486321}.
MUTAGEN 101 101 K->R: Not acetylated after
glucocorticoid-stimulation and no
increase of transactivation activity;
when associated with R-98 and R-102.
{ECO:0000269|PubMed:17301242}.
MUTAGEN 102 102 K->R: Not acetylated and no increase of
transactivation activity after
glucocorticoid-stimulation; when
associated with R-98 and R-101.
{ECO:0000269|PubMed:17301242}.
MUTAGEN 133 133 K->R: Not sumoylated. Decreases
ubiquitination and increases stability.
Loss of proliferation inhibition in T
cells. No effect on transactivation
activity. {ECO:0000269|PubMed:16585579,
ECO:0000269|PubMed:20194620,
ECO:0000269|PubMed:24061474}.
MUTAGEN 135 135 E->A: Not sumoylated and not
ubiquitinated.
{ECO:0000269|PubMed:20194620}.
MUTAGEN 179 179 T->A: Disruption of phosphorylation by
MAPK and GSK3B, acquisition of DNA-
binding activity and transactivation
function; when associated with A-184 and
A-188. {ECO:0000269|PubMed:15985551}.
MUTAGEN 180 180 S->A: Highly increases transactivation
activity; when associated with A-181.
{ECO:0000269|PubMed:19478079}.
MUTAGEN 181 181 S->A: Highly increases transactivation
activity; when associated with A-180.
{ECO:0000269|PubMed:19478079}.
MUTAGEN 184 184 S->A: Disruption of phosphorylation by
MAPK and GSK3B, acquisition of DNA-
binding activity and transactivation
function; when associated with A-179 and
A-188. {ECO:0000269|PubMed:15985551}.
MUTAGEN 188 188 T->A: Disruption of phosphorylation by
MAPK and GSK3B, acquisition of DNA-
binding activity and transactivation
function; when associated with A-179 and
A-184. {ECO:0000269|PubMed:15985551}.
MUTAGEN 215 215 K->R: No effect on transactivation
activity. {ECO:0000269|PubMed:18486321}.
MUTAGEN 217 217 T->A: Loss of hepatocyte proliferation
induction by TGFA.
{ECO:0000269|PubMed:10635333}.
MUTAGEN 217 217 T->E: Induces hepatocyte proliferation.
{ECO:0000269|PubMed:10635333}.
MUTAGEN 276 276 S->A: Reduces phosphorylation in response
to calcium. {ECO:0000269|PubMed:1314426}.
HELIX 240 282 {ECO:0000244|PDB:1CI6}.
SEQUENCE 296 AA; 31446 MW; 827AC4AFC209AE89 CRC64;
MHRLLAWDAA CLPPPPAAFR PMEVANFYYE PDCLAYGAKA ARAAPRAPAA EPAIGEHERA
IDFSPYLEPL APAADFAAPA PAHHDFLSDL FADDYGAKPS KKPADYGYVS LGRAGAKAAP
PACFPPPPPA ALKAEPGFEP ADCKRADDAP AMAAGFPFAL RAYLGYQATP SGSSGSLSTS
SSSSPPGTPS PADAKAAPAA CFAGPPAAPA KAKAKKTVDK LSDEYKMRRE RNNIAVRKSR
DKAKMRNLET QHKVLELTAE NERLQKKVEQ LSRELSTLRN LFKQLPEPLL ASAGHC


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