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

DNA damage-inducible transcript 3 protein (DDIT-3) (C/EBP zeta) (C/EBP-homologous protein) (CHOP) (C/EBP-homologous protein 10) (CHOP-10) (CCAAT/enhancer-binding protein homologous protein) (Growth arrest and DNA-damage-inducible protein GADD153)

 DDIT3_MOUSE             Reviewed;         168 AA.
P35639; Q91YW9;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-OCT-2017, entry version 144.
RecName: Full=DNA damage-inducible transcript 3 protein;
Short=DDIT-3;
AltName: Full=C/EBP zeta;
AltName: Full=C/EBP-homologous protein;
Short=CHOP;
AltName: Full=C/EBP-homologous protein 10;
Short=CHOP-10;
AltName: Full=CCAAT/enhancer-binding protein homologous protein;
AltName: Full=Growth arrest and DNA-damage-inducible protein GADD153;
Name=Ddit3; Synonyms=Chop, Chop10, Gadd153;
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], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=SWR/J;
PubMed=1547942; DOI=10.1101/gad.6.3.439;
Ron D., Habener J.F.;
"CHOP, a novel developmentally regulated nuclear protein that
dimerizes with transcription factors C/EBP and LAP and functions as a
dominant-negative inhibitor of gene transcription.";
Genes Dev. 6:439-453(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; 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).
[3]
PHOSPHORYLATION AT SER-78 AND SER-81.
PubMed=8650547; DOI=10.1126/science.272.5266.1347;
Wang X.Z., Ron D.;
"Stress-induced phosphorylation and activation of the transcription
factor CHOP (GADD153) by p38 MAP Kinase.";
Science 272:1347-1349(1996).
[4]
FUNCTION.
PubMed=12706815; DOI=10.1016/S0014-5793(03)00283-7;
Hattori T., Ohoka N., Hayashi H., Onozaki K.;
"C/EBP homologous protein (CHOP) up-regulates IL-6 transcription by
trapping negative regulating NF-IL6 isoform.";
FEBS Lett. 541:33-39(2003).
[5]
PHOSPHORYLATION AT SER-14; SER-15; SER-30 AND SER-31, AND MUTAGENESIS
OF SER-14; SER-15; SER-30 AND SER-31.
PubMed=12876286; DOI=10.1074/jbc.M306404200;
Ubeda M., Habener J.F.;
"CHOP transcription factor phosphorylation by casein kinase 2 inhibits
transcriptional activation.";
J. Biol. Chem. 278:40514-40520(2003).
[6]
FUNCTION.
PubMed=14684614; DOI=10.1210/en.2003-0868;
Pereira R.C., Delany A.M., Canalis E.;
"CCAAT/enhancer binding protein homologous protein (DDIT3) induces
osteoblastic cell differentiation.";
Endocrinology 145:1952-1960(2004).
[7]
FUNCTION.
PubMed=15601821; DOI=10.1101/gad.1250704;
Marciniak S.J., Yun C.Y., Oyadomari S., Novoa I., Zhang Y.,
Jungreis R., Nagata K., Harding H.P., Ron D.;
"CHOP induces death by promoting protein synthesis and oxidation in
the stressed endoplasmic reticulum.";
Genes Dev. 18:3066-3077(2004).
[8]
FUNCTION.
PubMed=15775988; DOI=10.1038/sj.emboj.7600596;
Ohoka N., Yoshii S., Hattori T., Onozaki K., Hayashi H.;
"TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP
pathway and is involved in cell death.";
EMBO J. 24:1243-1255(2005).
[9]
FUNCTION, AND INDUCTION.
PubMed=16670335; DOI=10.4049/jimmunol.176.10.6245;
Endo M., Mori M., Akira S., Gotoh T.;
"C/EBP homologous protein (CHOP) is crucial for the induction of
caspase-11 and the pathogenesis of lipopolysaccharide-induced
inflammation.";
J. Immunol. 176:6245-6253(2006).
[10]
FUNCTION, AND INDUCTION.
PubMed=19752026; DOI=10.1083/jcb.200904060;
Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R.,
Tabas I.;
"Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-
triphosphate receptor activity in endoplasmic reticulum stress-induced
apoptosis.";
J. Cell Biol. 186:783-792(2009).
[11]
INDUCTION.
PubMed=19855386; DOI=10.1038/ncb1996;
Woo C.W., Cui D., Arellano J., Dorweiler B., Harding H.,
Fitzgerald K.A., Ron D., Tabas I.;
"Adaptive suppression of the ATF4-CHOP branch of the unfolded protein
response by toll-like receptor signalling.";
Nat. Cell Biol. 11:1473-1480(2009).
[12]
FUNCTION, AND INDUCTION.
PubMed=19919955; DOI=10.1093/jb/mvp189;
Nakayama Y., Endo M., Tsukano H., Mori M., Oike Y., Gotoh T.;
"Molecular mechanisms of the LPS-induced non-apoptotic ER stress-CHOP
pathway.";
J. Biochem. 147:471-483(2010).
[13]
FUNCTION, AND INDUCTION.
PubMed=21159964; DOI=10.1523/JNEUROSCI.1598-10.2010;
Galehdar Z., Swan P., Fuerth B., Callaghan S.M., Park D.S.,
Cregan S.P.;
"Neuronal apoptosis induced by endoplasmic reticulum stress is
regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only
member PUMA.";
J. Neurosci. 30:16938-16948(2010).
[14]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH HDAC1.
PubMed=22242125; DOI=10.1371/journal.pone.0029498;
Alter J., Bengal E.;
"Stress-induced C/EBP homology protein (CHOP) represses MyoD
transcription to delay myoblast differentiation.";
PLoS ONE 6:E29498-E29498(2011).
[15]
FUNCTION.
PubMed=22265908; DOI=10.1161/CIRCULATIONAHA.111.041830;
Loinard C., Zouggari Y., Rueda P., Ramkhelawon B., Cochain C.,
Vilar J., Recalde A., Richart A., Charue D., Duriez M., Mori M.,
Arenzana-Seisdedos F., Levy B.I., Heymes C., Silvestre J.S.;
"C/EBP homologous protein-10 (CHOP-10) limits postnatal
neovascularization through control of endothelial nitric oxide
synthase gene expression.";
Circulation 125:1014-1026(2012).
-!- FUNCTION: Multifunctional transcription factor in ER stress
response. Plays an essential role in the response to a wide
variety of cell stresses and induces cell cycle arrest and
apoptosis in response to ER stress. Plays a dual role both as an
inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and
as an activator of other genes. Acts as a dominant-negative
regulator of C/EBP-induced transcription: dimerizes with members
of the C/EBP family, impairs their association with C/EBP binding
sites in the promoter regions, and inhibits the expression of
C/EBP regulated genes. Positively regulates the transcription of
TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA,
BCL2L11/BIM and ERO1L. Negatively regulates; expression of BCL2
and MYOD1, ATF4-dependent transcriptional activation of asparagine
synthetase (ASNS), CEBPA-dependent transcriptional activation of
hepcidin (HAMP) and CEBPB-mediated expression of peroxisome
proliferator-activated receptor gamma (PPARG). Inhibits the
canonical Wnt signaling pathway by binding to TCF7L2/TCF4,
impairing its DNA-binding properties and repressing its
transcriptional activity. Plays a regulatory role in the
inflammatory response through the induction of caspase-11
(CASP4/CASP11) which induces the activation of caspase-1 (CASP1)
and both these caspases increase the activation of pro-IL1B to
mature IL1B which is involved in the inflammatory response. Acts
as a major regulator of postnatal neovascularization through
regulation of endothelial nitric oxide synthase (NOS3)-related
signaling. {ECO:0000269|PubMed:12706815,
ECO:0000269|PubMed:14684614, ECO:0000269|PubMed:1547942,
ECO:0000269|PubMed:15601821, ECO:0000269|PubMed:15775988,
ECO:0000269|PubMed:16670335, ECO:0000269|PubMed:19752026,
ECO:0000269|PubMed:19919955, ECO:0000269|PubMed:21159964,
ECO:0000269|PubMed:22242125, ECO:0000269|PubMed:22265908}.
-!- SUBUNIT: Heterodimer. Interacts with TCF7L2/TCF4, EP300/P300,
HDAC5 and HDAC6. Interacts with TRIB3 which blocks its association
with EP300/P300. Interacts with FOXO3, CEBPB and ATF4 (By
similarity). Interacts with HDAC1. {ECO:0000250,
ECO:0000269|PubMed:22242125}.
-!- INTERACTION:
Q06507:Atf4; NbExp=3; IntAct=EBI-10636142, EBI-77383;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Present in the
cytoplasm under non-stressed conditions and ER stress leads to its
nuclear accumulation.
-!- INDUCTION: By oxidative stress, amino-acid deprivation, hypoxia
and ER stress. During ER stress, induced by a EIF2AK3/ATF4 pathway
and/or ERN1/ATF6 pathway. Expression is suppressed by TLR-TRIF
signaling pathway during prolonged ER stress.
{ECO:0000269|PubMed:16670335, ECO:0000269|PubMed:19752026,
ECO:0000269|PubMed:19855386, ECO:0000269|PubMed:19919955,
ECO:0000269|PubMed:21159964, ECO:0000269|PubMed:22242125}.
-!- DOMAIN: The N-terminal region is necessary for its proteasomal
degradation, transcriptional activity and interaction with
EP300/P300. {ECO:0000250}.
-!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
{ECO:0000250}.
-!- PTM: Phosphorylation at serine residues by MAPK14 enhances its
transcriptional activation activity while phosphorylation at
serine residues by CK2 inhibits its transcriptional activation
activity. {ECO:0000269|PubMed:12876286,
ECO:0000269|PubMed:8650547}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X67083; CAA47465.1; -; mRNA.
EMBL; BC013718; AAH13718.1; -; mRNA.
CCDS; CCDS24236.1; -.
PIR; S26148; S26148.
RefSeq; NP_001277112.1; NM_001290183.1.
RefSeq; NP_031863.3; NM_007837.4.
RefSeq; XP_006513260.1; XM_006513197.3.
UniGene; Mm.110220; -.
ProteinModelPortal; P35639; -.
SMR; P35639; -.
BioGrid; 199078; 2.
DIP; DIP-60705N; -.
IntAct; P35639; 1.
STRING; 10090.ENSMUSP00000026475; -.
BindingDB; P35639; -.
ChEMBL; CHEMBL2146304; -.
iPTMnet; P35639; -.
PhosphoSitePlus; P35639; -.
MaxQB; P35639; -.
PaxDb; P35639; -.
PRIDE; P35639; -.
Ensembl; ENSMUST00000026475; ENSMUSP00000026475; ENSMUSG00000025408.
GeneID; 13198; -.
KEGG; mmu:13198; -.
UCSC; uc007hiy.2; mouse.
CTD; 1649; -.
MGI; MGI:109247; Ddit3.
eggNOG; ENOG410ISXY; Eukaryota.
eggNOG; ENOG41127XB; LUCA.
GeneTree; ENSGT00390000006305; -.
HOGENOM; HOG000089934; -.
HOVERGEN; HBG051328; -.
InParanoid; P35639; -.
KO; K04452; -.
OMA; WELEAWY; -.
OrthoDB; EOG091G0UKC; -.
PhylomeDB; P35639; -.
TreeFam; TF105006; -.
PRO; PR:P35639; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000025408; -.
CleanEx; MM_DDIT3; -.
ExpressionAtlas; P35639; baseline and differential.
Genevisible; P35639; MM.
GO; GO:1990622; C:CHOP-ATF3 complex; ISO:MGI.
GO; GO:1990617; C:CHOP-ATF4 complex; ISO:MGI.
GO; GO:0036488; C:CHOP-C/EBP complex; IPI:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005770; C:late endosome; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
GO; GO:0008140; F:cAMP response element binding protein binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0043522; F:leucine zipper domain binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IMP:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0001955; P:blood vessel maturation; IMP:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
GO; GO:0045454; P:cell redox homeostasis; ISO:MGI.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:MGI.
GO; GO:0006983; P:ER overload response; IMP:MGI.
GO; GO:0072655; P:establishment of protein localization to mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
GO; GO:1990442; P:intrinsic apoptotic signaling pathway in response to nitrosative stress; IDA:ParkinsonsUK-UCL.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0032792; P:negative regulation of CREB transcription factor activity; ISO:MGI.
GO; GO:2000016; P:negative regulation of determination of dorsal identity; IDA:BHF-UCL.
GO; GO:0043392; P:negative regulation of DNA binding; IGI:ParkinsonsUK-UCL.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IGI:MGI.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:ParkinsonsUK-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:1901216; P:positive regulation of neuron death; IMP:ParkinsonsUK-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:ParkinsonsUK-UCL.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0051259; P:protein oligomerization; ISO:MGI.
GO; GO:0044324; P:regulation of transcription involved in anterior/posterior axis specification; IDA:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:0042594; P:response to starvation; IDA:UniProtKB.
GO; GO:0006986; P:response to unfolded protein; ISO:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
InterPro; IPR016670; DNA_damage_induc_transcript_3.
PANTHER; PTHR16833; PTHR16833; 1.
PIRSF; PIRSF016571; C/EBPzeta_CHOP_DDIT3; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Activator; Apoptosis; Cell cycle; Complete proteome; Cytoplasm;
DNA-binding; Growth arrest; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Stress response; Transcription;
Transcription regulation; Ubl conjugation; Unfolded protein response;
Wnt signaling pathway.
CHAIN 1 168 DNA damage-inducible transcript 3
protein.
/FTId=PRO_0000076643.
DOMAIN 98 161 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 10 26 N-terminal. {ECO:0000250}.
REGION 10 18 Interaction with TRIB3. {ECO:0000250}.
REGION 100 129 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 133 147 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 92 97 Poly-Glu.
MOD_RES 14 14 Phosphoserine; by CK2.
{ECO:0000269|PubMed:12876286}.
MOD_RES 15 15 Phosphoserine; by CK2.
{ECO:0000269|PubMed:12876286}.
MOD_RES 30 30 Phosphoserine; by CK2.
{ECO:0000269|PubMed:12876286}.
MOD_RES 31 31 Phosphoserine; by CK2.
{ECO:0000269|PubMed:12876286}.
MOD_RES 78 78 Phosphoserine; by MAPK14.
{ECO:0000269|PubMed:8650547}.
MOD_RES 81 81 Phosphoserine; by MAPK14.
{ECO:0000269|PubMed:8650547}.
MUTAGEN 14 14 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:12876286}.
MUTAGEN 15 15 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:12876286}.
MUTAGEN 30 30 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:12876286}.
MUTAGEN 31 31 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:12876286}.
CONFLICT 34 34 I -> N (in Ref. 2; AAH13718).
{ECO:0000305}.
SEQUENCE 168 AA; 19189 MW; CA423B79512F33AB CRC64;
MAAESLPFTL ETVSSWELEA WYEDLQEVLS SDEIGGTYIS SPGNEEEESK TFTTLDPASL
AWLTEEPGPT EVTRTSQSPR SPDSSQSSMA QEEEEEEQGR TRKRKQSGQC PARPGKQRMK
EKEQENERKV AQLAEENERL KQEIERLTRE VETTRRALID RMVSLHQA


Related products :

Catalog number Product name Quantity
EIAAB10727 Bos taurus,Bovine,C_EBP-homologous protein,C_EBP-homologous protein 10,CHOP,CHOP,CHOP10,CHOP-10,DDIT3,DDIT-3,DNA damage-inducible transcript 3 protein,GADD153,Growth arrest and DNA-damage-inducible pr
EIAAB10726 C_EBP-homologous protein,C_EBP-homologous protein 10,CHOP,Chop,Chop10,CHOP-10,Ddit3,DDIT-3,DNA damage-inducible transcript 3 protein,Gadd153,Growth arrest and DNA-damage-inducible protein GADD153,Mous
EIAAB10729 C_EBP-homologous protein,C_EBP-homologous protein 10,CHOP,CHOP,CHOP10,CHOP-10,DDIT3,DDIT-3,DNA damage-inducible transcript 3 protein,GADD153,Growth arrest and DNA damage-inducible protein GADD153,Homo
EIAAB10728 C_EBP-homologous protein,C_EBP-homologous protein 10,CHOP,Chop,Chop10,CHOP-10,Ddit3,DDIT-3,DNA damage-inducible transcript 3 protein,Gadd153,Growth arrest and DNA-damage-inducible protein GADD153,Rat,
20-272-190514 GADD153 - Mouse monoclonal [9C8] to GADD153; DDIT-3; Growth arrest and DNA-damage-inducible protein GADD153; C_EBP-homologous protein; CHOP Monoclonal 0.05 mg
18-272-195087 DDIT3 - Rabbit polyclonal to DDIT3; DDIT-3; Growth arrest and DNA-damage-inducible protein GADD153; C_EBP-homologous protein; CHOP Polyclonal 0.1 ml
EIAAB10733 Ddit4,Dexamethasone-induced gene 2 protein,Dig2,DNA damage-inducible transcript 4 protein,HIF-1 responsive protein RTP801,Mouse,Mus musculus,Protein regulated in development and DNA damage response 1,
EIAAB10743 DDIT4L,DNA damage-inducible transcript 4-like protein,HIF-1 responsive protein RTP801-like,Homo sapiens,Human,Protein regulated in development and DNA damage response 2,REDD2,REDD-2,RTP801L
bs-1361P Peptides: GADD153(Growth arrest and DNA damage-inducible 153) Protein Length:12-25 amino acids. 200ug lyophilized
EIAAB10730 Ddit4,DNA damage-inducible transcript 4 protein,HIF-1 responsive protein RTP801,Protein regulated in development and DNA damage response 1,Rat,Rattus norvegicus,Redd1,REDD-1,Rtp801
EIAAB10732 DDIT4,DNA damage-inducible transcript 4 protein,HIF-1 responsive protein RTP801,Homo sapiens,Human,Protein regulated in development and DNA damage response 1,REDD1,REDD-1,RTP801
10-288-22011F Growth arrest and DNA-damage-inducible protein GADD45 gamma - Cytokine-responsive protein CR6 0.05 mg
10-288-22011F Growth arrest and DNA-damage-inducible protein GADD45 gamma - Cytokine-responsive protein CR6 0.1 mg
15-288-22011 Growth arrest and DNA-damage-inducible protein GADD45 gamma - Cytokine-responsive protein CR6 Polyclonal 0.1 mg
15-288-22011 Growth arrest and DNA-damage-inducible protein GADD45 gamma - Cytokine-responsive protein CR6 Polyclonal 0.05 mg
GADD45GIP1-1280H Protein Recombinant Human Growth Arrest And DNA-Damage-Inducible, Gamma Interacting Protein 1, His-tagged 50ug
GADD45GIP1-1280H Protein: Recombinant Human Growth Arrest And DNA-Damage-Inducible, Gamma Interacting Protein 1, His-tagged 50ug
EIAAB32159 Gadd34,Growth arrest and DNA damage-inducible protein GADD34,Myd116,Myeloid differentiation primary response protein MyD116 homolog,Peg3,PEG-3,Ppp1r15a,Progression elevated gene 3 protein,Protein phos
EIAAB32161 GADD34,Growth arrest and DNA damage-inducible protein GADD34,Homo sapiens,Human,Myeloid differentiation primary response protein MyD116 homolog,PPP1R15A,Protein phosphatase 1 regulatory subunit 15A
EIAAB41165 Mouse,Mus musculus,p53-dependent damage-inducible nuclear protein 1,p53DINP1,Sip,Stress-induced protein,TEAP,Thymus-expressed acidic protein,Trp53inp1,Tumor protein p53-inducible nuclear protein 1
EIAAB41166 p53-dependent damage-inducible nuclear protein 1,p53DINP1,Rat,Rattus norvegicus,Sip,Stress-induced protein,TEAP,Thymus-expressed acidic protein,Trp53inp1,Tumor protein p53-inducible nuclear protein 1
EIAAB10707 Damage-specific DNA-binding protein 1,DDB p127 subunit,DDB1,DDBa,DNA damage-binding protein 1,DNA damage-binding protein a,HBV X-associated protein 1,Homo sapiens,Human,UV-damaged DNA-binding factor,U
EIAAB32158 Gadd34,Growth arrest and DNA damage-inducible protein GADD34,Mouse,Mus musculus,Myd116,Myeloid differentiation primary response protein MyD116,Ppp1r15a,Protein phosphatase 1 regulatory subunit 15A
EIAAB10746 Ddit4l,DNA damage-inducible transcript 4-like protein,HIF-1 responsive protein RTP801-like,Mouse,Mus musculus,Rtp801l,Smhs1,Soleus muscle atrophied after hindlimb suspension protein 1
PC-GADD34 Growth arrest & DNA damage-inducible protein, WB control 100-150ul


 

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