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

Cyclic AMP-responsive element-binding protein 3-like protein 1 (cAMP-responsive element-binding protein 3-like protein 1) (Old astrocyte specifically-induced substance) (OASIS) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 1 (Oasis N-terminal fragment) (OA-N)]

 CR3L1_MOUSE             Reviewed;         519 AA.
Q9Z125; Q91W70;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 2.
25-OCT-2017, entry version 124.
RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 1;
Short=cAMP-responsive element-binding protein 3-like protein 1;
AltName: Full=Old astrocyte specifically-induced substance {ECO:0000303|PubMed:10350641};
Short=OASIS {ECO:0000303|PubMed:10350641};
Contains:
RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 1;
AltName: Full=Oasis N-terminal fragment {ECO:0000303|PubMed:19767743};
Short=OA-N {ECO:0000303|PubMed:19767743};
Name=Creb3l1; Synonyms=Oasis;
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 2), TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND INDUCTION.
STRAIN=ICR;
PubMed=10350641; DOI=10.1016/S0169-328X(99)00102-3;
Honma Y., Kanazawa K., Mori T., Tanno Y., Tojo M., Kiyosawa H.,
Takeda J., Nikaido T., Tsukamoto T., Yokoya S., Wanaka A.;
"Identification of a novel gene, OASIS, which encodes for a putative
CREB/ATF family transcription factor in the long-term cultured
astrocytes and gliotic tissue.";
Brain Res. Mol. Brain Res. 69:93-103(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Salivary 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).
[4]
FUNCTION AS TRANSCRIPTION ACTIVATOR, BINDING TO CRE CONSENSUS
SEQUENCE, INDUCTION, AND IDENTIFICATION OF THE TRANSACTIVATION DOMAIN.
PubMed=12480185; DOI=10.1016/S0169-328X(02)00521-1;
Nikaido T., Iseki K., Mori T., Takaki H., Yokoya S., Hagino S.,
Takeda J., Zhang Y., Takeuchi M., Kikuchi S., Wanaka A.;
"Expression of OASIS, a CREB/ATF family transcription factor, in CNS
lesion and its transcriptional activity.";
Brain Res. Mol. Brain Res. 108:129-138(2002).
[5]
DEVELOPMENTAL STAGE.
PubMed=12684764; DOI=10.1007/s00429-003-0311-z;
Hikake T., Mori T., Iseki K., Hagino S., Zhang Y., Takagi H.,
Yokoya S., Wanaka A.;
"Comparison of expression patterns between CREB family transcription
factor OASIS and proteoglycan core protein genes during murine tooth
development.";
Anat. Embryol. (Berl.) 206:373-380(2003).
[6]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY ER STRESS, GLYCOSYLATION,
AND MUTAGENESIS OF PRO-392; ARG-423 AND LEU-426.
PubMed=15665855; DOI=10.1038/ncb1213;
Kondo S., Murakami T., Tatsumi K., Ogata M., Kanemoto S., Otori K.,
Iseki K., Wanaka A., Imaizumi K.;
"OASIS, a CREB/ATF-family member, modulates UPR signalling in
astrocytes.";
Nat. Cell Biol. 7:186-194(2005).
[7]
FUNCTION IN OSTEOGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
INDUCTION BY BMP2 AND RUNX2, CLEAVAGE UPON ER STRESS, AND DISRUPTION
PHENOTYPE.
PubMed=19767743; DOI=10.1038/ncb1963;
Murakami T., Saito A., Hino S., Kondo S., Kanemoto S., Chihara K.,
Sekiya H., Tsumagari K., Ochiai K., Yoshinaga K., Saitoh M.,
Nishimura R., Yoneda T., Kou I., Furuichi T., Ikegawa S., Ikawa M.,
Okabe M., Wanaka A., Imaizumi K.;
"Signalling mediated by the endoplasmic reticulum stress transducer
OASIS is involved in bone formation.";
Nat. Cell Biol. 11:1205-1211(2009).
[8]
UBIQUITINATION.
PubMed=22705851; DOI=10.1038/cdd.2012.77;
Kondo S., Hino S.I., Saito A., Kanemoto S., Kawasaki N., Asada R.,
Izumi S., Iwamoto H., Oki M., Miyagi H., Kaneko M., Nomura Y.,
Urano F., Imaizumi K.;
"Activation of OASIS family, ER stress transducers, is dependent on
its stabilization.";
Cell Death Differ. 19:1939-1949(2012).
-!- FUNCTION: Transcription factor involved in unfolded protein
response (UPR). Binds the DNA consensus sequence 5'-GTGXGCXGC-3'
(By similarity). In the absence of endoplasmic reticulum (ER)
stress, inserted into ER membranes, with N-terminal DNA-binding
and transcription activation domains oriented toward the cytosolic
face of the membrane. In response to ER stress, transported to the
Golgi, where it is cleaved in a site-specific manner by resident
proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal
cytosolic domain is translocated to the nucleus to effect
transcription of specific target genes. Plays a critical role in
bone formation through the transcription of COL1A1, and possibly
COL1A2, and the secretion of bone matrix proteins. Directly binds
to the UPR element (UPRE)-like sequence in an osteoblast-specific
COL1A1 promoter region and induces its transcription. Does not
regulate COL1A1 in other tissues, such as skin (PubMed:19767743).
Required to protect astrocytes from ER stress-induced cell death.
In astrocytes, binds to the cAMP response element (CRE) of the
BiP/HSPA5 promoter and participate in its transcriptional
activation (PubMed:15665855). Inhibits cell-cycle progression by
binding to promoters and activating transcription of genes
encoding cell-cycle inhibitors, such as p21/CDKN1A (By
similarity). Required for TGFB1 to activate genes involved in the
assembly of collagen extracellular matrix (By similarity).
{ECO:0000250|UniProtKB:Q96BA8, ECO:0000269|PubMed:12480185,
ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}.
-!- SUBUNIT: Interacts with SMAD4, the interaction takes place upon
TGFB1 induction and SMAD4 acts as CREB3L1 coactivator to induce
the expression of genes involved in assembly of collagen
extracellular matrix. {ECO:0000250|UniProtKB:Q96BA8}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743};
Single-pass type II membrane protein
{ECO:0000269|PubMed:15665855}. Note=ER membrane resident protein.
Upon ER stress, translocated to the Golgi apparatus where it is
cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-
responsive element-binding protein 3-like protein 1) is
transported into the nucleus. {ECO:0000269|PubMed:15665855,
ECO:0000269|PubMed:19767743}.
-!- SUBCELLULAR LOCATION: Processed cyclic AMP-responsive element-
binding protein 3-like protein 1: Nucleus
{ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}.
Note=Upon ER stress, transported into the nucleus.
{ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Z125-1; Sequence=Displayed;
Name=2;
IsoId=Q9Z125-2; Sequence=VSP_025633;
-!- TISSUE SPECIFICITY: Expressed in cortical and trabecular bones.
Highly expressed in osteoblasts, but not detected in osteoclasts,
nor in macrophages (PubMed:19767743). Expressed at relatively low
levels in lung and kidney. Weakly expressed in brain and spleen.
{ECO:0000269|PubMed:10350641, ECO:0000269|PubMed:19767743}.
-!- DEVELOPMENTAL STAGE: In the embryo, primarily expressed in the
cartilage, tooth germs and salivary gland. Expressed in the inner
enamel epithelium during the cap and bell stages (14.5 dpc - 18.5
dpc), in the preodontoblasts during differentiation stage (18.5
dpc - P0) and in the differentiating odontoblasts during the early
secretory stage (P2.5-P4.5). After birth, at P14, detected at low
levels in the cerebral cortex, hippocampus and thalamus. In the
adult brain, expression becomes weaker.
{ECO:0000269|PubMed:10350641, ECO:0000269|PubMed:12684764}.
-!- INDUCTION: Up-regulated in astrocytes residing in or close to CNS
lesions, such as cryo-injured cerebral cortex and stab-injured
spinal cord (PubMed:12480185, PubMed:15665855). Up-regulated by ER
stress in astrocytes (at protein level). This induction is
accompanied by increased proteolytic cleavage that releases the N-
terminal transcription factor domain (PubMed:15665855). Up-
regulated by BMP2 and RUNX2 in calvaria osteoblasts. This
induction at the transcript and protein levels is accompanied by
increased proteolytic cleavage that releases the N-terminal
transcription factor domain, possibly through mild ER stress
(PubMed:19767743). Also induced by BMP2 in bone marrow stromal
cells. {ECO:0000269|PubMed:10350641, ECO:0000269|PubMed:12480185,
ECO:0000269|PubMed:15665855, ECO:0000269|PubMed:19767743}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:15665855}.
-!- PTM: Ubiquitinated by HRD1/SYVN1; undergoes 'Lys-48'-linked
ubiquitination, followed by rapid proteasomal degradation under
normal conditions. Upon ER stress, SYVN1 E3 ubiquitin-protein
ligase dissociates from its substrate, ubiquitination does not
occur and CREB3L1 is stabilized. {ECO:0000269|PubMed:22705851}.
-!- PTM: Upon ER stress, translocated to the Golgi apparatus, where it
is processed by regulated intramembrane proteolysis (RIP) to
release the cytosol-facing N-terminal transcription factor domain
(PubMed:19767743). The cleavage is performed sequentially by site-
1 and site-2 proteases (S1P/MBTPS1 and S2P/MBTPS2). RIP is induced
by TGFB1 and ceramide. {ECO:0000250|UniProtKB:Q96BA8,
ECO:0000269|PubMed:19767743}.
-!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected
Mendelian rate, but show growth retardation. They exhibit severe
osteopenia, involving a decrease in type I collagen in the bone
matrix and a decline in the activity of osteoblasts. Osteoblasts
show abnormally expanded rough endoplasmic reticulum, containing
of a large amount of bone matrix proteins, including COL1A1 and
osteocalcin/BGLAP. {ECO:0000269|PubMed:19767743}.
-!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB017614; BAA75670.1; -; mRNA.
EMBL; AL732484; CAM22585.1; -; Genomic_DNA.
EMBL; BC016447; AAH16447.1; -; mRNA.
RefSeq; NP_036087.2; NM_011957.2.
UniGene; Mm.10353; -.
ProteinModelPortal; Q9Z125; -.
SMR; Q9Z125; -.
BioGrid; 204979; 1.
STRING; 10090.ENSMUSP00000028663; -.
PhosphoSitePlus; Q9Z125; -.
PaxDb; Q9Z125; -.
PRIDE; Q9Z125; -.
GeneID; 26427; -.
KEGG; mmu:26427; -.
UCSC; uc008kxf.1; mouse. [Q9Z125-2]
CTD; 90993; -.
MGI; MGI:1347062; Creb3l1.
eggNOG; KOG0709; Eukaryota.
eggNOG; ENOG410ZZQM; LUCA.
HOGENOM; HOG000060150; -.
HOVERGEN; HBG057480; -.
InParanoid; Q9Z125; -.
KO; K09048; -.
PhylomeDB; Q9Z125; -.
TreeFam; TF316079; -.
Reactome; R-MMU-8874211; CREB3 factors activate genes.
ChiTaRS; Creb3l1; mouse.
PRO; PR:Q9Z125; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CREB3L1; -.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0035497; F:cAMP response element binding; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:MGI.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:UniProtKB.
GO; GO:0070278; P:extracellular matrix constituent secretion; IDA:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0001649; P:osteoblast differentiation; IMP:UniProtKB.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:UniProtKB.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
GO; GO:0030278; P:regulation of ossification; IMP:MGI.
Gene3D; 1.10.880.10; -; 1.
InterPro; IPR004827; bZIP.
InterPro; IPR001630; Leuzip_CREB.
InterPro; IPR029805; OASIS.
InterPro; IPR008917; TF_DNA-bd.
PANTHER; PTHR22952:SF24; PTHR22952:SF24; 1.
Pfam; PF00170; bZIP_1; 1.
PRINTS; PR00041; LEUZIPPRCREB.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome;
Developmental protein; DNA-binding; Endoplasmic reticulum;
Glycoprotein; Isopeptide bond; Membrane; Nucleus; Reference proteome;
Signal-anchor; Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Ubl conjugation; Unfolded protein response.
CHAIN 1 519 Cyclic AMP-responsive element-binding
protein 3-like protein 1.
/FTId=PRO_0000288065.
CHAIN 1 ? Processed cyclic AMP-responsive element-
binding protein 3-like protein 1.
/FTId=PRO_0000296207.
TOPO_DOM 1 376 Cytoplasmic. {ECO:0000255}.
TRANSMEM 377 397 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 398 519 Lumenal. {ECO:0000255}.
DOMAIN 290 353 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 60 Required for transcription activation.
{ECO:0000250|UniProtKB:Q96BA8}.
REGION 292 321 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 332 353 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 392 395 S2P recognition.
{ECO:0000250|UniProtKB:Q96BA8}.
MOTIF 423 426 S1P recognition.
{ECO:0000250|UniProtKB:Q96BA8}.
SITE 426 427 Cleavage; by S1P. {ECO:0000250}.
CARBOHYD 493 493 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 184 184 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96BA8}.
VAR_SEQ 503 519 EWFHDRDLGPNTTIKLS -> KGVVP (in isoform
2). {ECO:0000303|PubMed:10350641}.
/FTId=VSP_025633.
MUTAGEN 392 392 P->L: Loss of proteolytic cleavage; when
associated with V-423 and V-426.
{ECO:0000269|PubMed:15665855}.
MUTAGEN 423 423 R->A: Loss of proteolytic cleavage; when
associated with L-392 and V-426.
{ECO:0000269|PubMed:15665855}.
MUTAGEN 426 426 L->V: Loss of proteolytic cleavage; when
associated with L-392 and A-423.
{ECO:0000269|PubMed:15665855}.
SEQUENCE 519 AA; 56959 MW; 9DCB22B9B28DA2E8 CRC64;
MDAVLEPFPA DRLFPGSSFL DLGDLNESDF LNNAHFPEHL DHFVENMEDF SNDLFSSFFD
DPVLDEKSAL LDMELDSPAP GIQAEHSYSL SGDSAPQSPL VPVKMEDTTQ DVEHGAWALG
NKLCSIMVKQ EQSPELPVDP LAASSAMAAA AAMATPPLLG LSPMPRLPIP HQAPGEMTQL
PVIKAEPPEM SQFLKVTPED LVQMPPTPPS SHGSDSDGSQ SPRSLPPSSP VRPMARSSTA
ISTSPLLTAP HKLQGTSGPL LLTEEEKRTL IAEGYPIPTK LPLTKAEEKA LKRVRRKIKN
KISAQESRRK KKEYVECLEK KVETYTSENN ELWKKVETLE TANRTLLQQL QKLQTLVTSK
ISRPYKMAAT QTGTCLMVAA LCFVLVLGSL VPCLPAFSSG SMTVKEDPIA ADSVYAASQM
PSRSLLFYDD GAGSWEDGRG ALLPVEPPEG WELKPGGPAE QRPQDHLRHD RADSIHETTK
YLRETWPEDT DDNGTSPNFS HPEWFHDRDL GPNTTIKLS


Related products :

Catalog number Product name Quantity
EIAAB09237 cAMP-responsive element-binding protein 3-like protein 1,Creb3l1,Cyclic AMP-responsive element-binding protein 3-like protein 1,OASIS,Oasis,Old astrocyte specifically-induced substance,Rat,Rattus norv
EIAAB09238 cAMP-responsive element-binding protein 3-like protein 1,CREB3L1,Cyclic AMP-responsive element-binding protein 3-like protein 1,Homo sapiens,Human,OASIS,OASIS,Old astrocyte specifically-induced substa
EIAAB09236 cAMP-responsive element-binding protein 3-like protein 1,Creb3l1,Cyclic AMP-responsive element-binding protein 3-like protein 1,Mouse,Mus musculus,OASIS,Oasis,Old astrocyte specifically-induced substa
EIAAB09247 AIbZIP,Aibzip,Androgen-induced basic leucine zipper protein,cAMP-responsive element-binding protein 3-like protein 4,Creb3l4,Cyclic AMP-responsive element-binding protein 3-like protein 4,Rat,Rattus n
U1318b CLIA Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
E1318b ELISA kit Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
E1318b ELISA Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
EIAAB09243 cAMP-responsive element-binding protein 3-like protein 3,CREB3L3,CREBH,Cyclic AMP-responsive element-binding protein 3-like protein 3,Homo sapiens,Human,HYST1481,Transcription factor CREB-H
EIAAB09244 cAMP-responsive element-binding protein 3-like protein 3,Creb3l3,Crebh,Cyclic AMP-responsive element-binding protein 3-like protein 3,Mouse,Mus musculus,Transcription factor CREB-H
EIAAB09242 cAMP-responsive element-binding protein 3-like protein 3,Creb3l3,Cyclic AMP-responsive element-binding protein 3-like protein 3,Rat,Rattus norvegicus,Transcription factor CREB-H
EIAAB09240 Bbf2h7,cAMP-responsive element-binding protein 3-like protein 2,Creb3l2,Cyclic AMP-responsive element-binding protein 3-like protein 2,Mouse,Mus musculus
E1318h ELISA cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
U1318h CLIA cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
EIAAB09321 cAMP-responsive element-binding protein 5,CREB5,CREB-5,CREBPA,CRE-BPa,Cyclic AMP-responsive element-binding protein 5,Homo sapiens,Human
E1318h ELISA kit cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
EIAAB09318 Bos taurus,Bovine,cAMP-responsive element-binding protein 3,CREB3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Luman
EIAAB09239 BBF2 human homolog on chromosome 7,BBF2H7,cAMP-responsive element-binding protein 3-like protein 2,CREB3L2,Cyclic AMP-responsive element-binding protein 3-like protein 2,Homo sapiens,Human
EIAAB09245 Bos taurus,Bovine,cAMP-responsive element-binding protein 3-like protein 3,CREB3L3,Cyclic AMP-responsive element-binding protein 3-like protein 3
EIAAB09322 cAMP-responsive element-binding protein 5,Creb5,CREB-5,CRE-BPa,Cyclic AMP-responsive element-binding protein 5,Mouse,Mus musculus
EIAAB09246 Acre1,ATCE1,Atce1,Attaching to CRE-like 1,cAMP-responsive element-binding protein 3-like protein 4,Creb3l4,Cyclic AMP-responsive element-binding protein 3-like protein 4,Jal,mJAL,Mouse,Mus musculus,Ti
EIAAB09241 cAMP-responsive element-binding protein 3-like protein 2,Creb3l2,Cyclic AMP-responsive element-binding protein 3-like protein 2,Ra69,Rat,Rattus norvegicus,SCI-related protein Ra69
EIAAB09320 cAMP-responsive element-binding protein 3,CREB3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Homo sapiens,Human,Luman,LZIP,Transcription factor LZIP-alpha
EIAAB09319 cAMP-responsive element-binding protein 3,Creb3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Lzip,Mouse,Mus musculus,Transcription factor LZIP
E1318r ELISA cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Rat,Rattus norvegicus 96T
E1318m ELISA kit cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Mouse,Mus musculus 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