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CREB binding protein

 A0A1D5PPD0_CHICK        Unreviewed;      2522 AA.
A0A1D5PPD0;
30-NOV-2016, integrated into UniProtKB/TrEMBL.
10-APR-2019, sequence version 2.
17-JUN-2020, entry version 31.
SubName: Full=CREB binding protein {ECO:0000313|Ensembl:ENSGALP00000054729};
Name=CREBBP {ECO:0000313|Ensembl:ENSGALP00000054729};
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
Phasianinae; Gallus.
NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000054729, ECO:0000313|Proteomes:UP000000539};
[1] {ECO:0000313|Ensembl:ENSGALP00000054729, ECO:0000313|Proteomes:UP000000539}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000054729,
ECO:0000313|Proteomes:UP000000539};
PubMed=15592404; DOI=10.1038/nature03154;
International Chicken Genome Sequencing Consortium;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide unique
perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
[2] {ECO:0000313|Ensembl:ENSGALP00000054729}
IDENTIFICATION.
STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000054729};
Ensembl;
Submitted (OCT-2016) to UniProtKB.
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EMBL; AADN05000376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
Ensembl; ENSGALT00000065134; ENSGALP00000054729; ENSGALG00000007762.
GeneTree; ENSGT00940000155364; -.
OrthoDB; 236283at2759; -.
Reactome; R-GGA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-GGA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-GGA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-GGA-350054; Notch-HLH transcription pathway.
Reactome; R-GGA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
Reactome; R-GGA-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
Reactome; R-GGA-8941856; RUNX3 regulates NOTCH signaling.
Reactome; R-GGA-9018519; Estrogen-dependent gene expression.
Reactome; R-GGA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-GGA-9617629; Regulation of FOXO transcriptional activity by acetylation.
Proteomes; UP000000539; Chromosome 14.
ExpressionAtlas; A0A1D5PPD0; baseline and differential.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
GO; GO:0016604; C:nuclear body; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0043426; F:MRF binding; IEA:Ensembl.
GO; GO:0002039; F:p53 binding; IEA:Ensembl.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
GO; GO:1990258; P:histone glutamine methylation; IEA:Ensembl.
GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
CDD; cd15802; RING_CBP-p300; 1.
Gene3D; 1.10.1630.10; -; 1.
Gene3D; 1.10.246.20; -; 1.
Gene3D; 1.20.1020.10; -; 2.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 2.10.110.40; -; 1.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.30.60.90; -; 1.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR031162; CBP_P300_HAT.
InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
InterPro; IPR003101; KIX_dom.
InterPro; IPR036529; KIX_dom_sf.
InterPro; IPR009110; Nuc_rcpt_coact.
InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
InterPro; IPR010303; RING_CBP-p300.
InterPro; IPR038547; RING_CBP-p300_sf.
InterPro; IPR035898; TAZ_dom_sf.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR000197; Znf_TAZ.
InterPro; IPR000433; Znf_ZZ.
InterPro; IPR043145; Znf_ZZ_sf.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF09030; Creb_binding; 1.
Pfam; PF06001; DUF902; 1.
Pfam; PF08214; HAT_KAT11; 1.
Pfam; PF02172; KIX; 1.
Pfam; PF02135; zf-TAZ; 2.
Pfam; PF00569; ZZ; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SMART; SM01250; KAT11; 1.
SMART; SM00551; ZnF_TAZ; 2.
SMART; SM00291; ZnF_ZZ; 1.
SUPFAM; SSF47040; SSF47040; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57933; SSF57933; 2.
SUPFAM; SSF69125; SSF69125; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51727; CBP_P300_HAT; 1.
PROSITE; PS50952; KIX; 1.
PROSITE; PS50134; ZF_TAZ; 2.
PROSITE; PS01357; ZF_ZZ_1; 1.
PROSITE; PS50135; ZF_ZZ_2; 1.
4: Predicted;
Acyltransferase {ECO:0000256|PROSITE-ProRule:PRU01065};
Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035,
ECO:0000256|SAAS:SAAS00979529};
Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00203,
ECO:0000256|SAAS:SAAS01261576};
Reference proteome {ECO:0000313|Proteomes:UP000000539};
Transferase {ECO:0000256|PROSITE-ProRule:PRU01065};
Zinc {ECO:0000256|PROSITE-ProRule:PRU00203, ECO:0000256|SAAS:SAAS01261576};
Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00203,
ECO:0000256|SAAS:SAAS01261576}.
DOMAIN 350..436
/note="TAZ-type"
/evidence="ECO:0000259|PROSITE:PS50134"
DOMAIN 589..668
/note="KIX"
/evidence="ECO:0000259|PROSITE:PS50952"
DOMAIN 1117..1189
/note="Bromo"
/evidence="ECO:0000259|PROSITE:PS50014"
DOMAIN 1337..1714
/note="CBP/p300-type HAT"
/evidence="ECO:0000259|PROSITE:PS51727"
DOMAIN 1715..1758
/note="ZZ-type"
/evidence="ECO:0000259|PROSITE:PS50135"
DOMAIN 1779..1860
/note="TAZ-type"
/evidence="ECO:0000259|PROSITE:PS50134"
ZN_FING 350..436
/note="TAZ-type"
/evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
ZN_FING 1779..1860
/note="TAZ-type"
/evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
REGION 1..23
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 74..152
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 444..483
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 495..519
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 845..1101
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1265..1284
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1448..1450
/note="Acetyl-CoA binding"
/evidence="ECO:0000256|PROSITE-ProRule:PRU01065"
REGION 1460..1461
/note="Acetyl-CoA binding"
/evidence="ECO:0000256|PROSITE-ProRule:PRU01065"
REGION 1570..1629
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1888..1985
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 2138..2162
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 2228..2281
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 2314..2440
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 74..115
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 121..152
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 444..482
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 845..887
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 888..902
/note="Pro-rich"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 903..947
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 959..1007
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1012..1079
/note="Polyampholyte"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1080..1095
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1570..1585
/note="Polyampholyte"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1602..1616
/note="Basic"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1888..1909
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1910..1930
/note="Pro-rich"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1931..1952
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1954..1968
/note="Pro-rich"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 2250..2281
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 2314..2370
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 2371..2398
/note="Pro-rich"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 2415..2440
/note="Polar"
/evidence="ECO:0000256|SAM:MobiDB-lite"
BINDING 1507
/note="Acetyl-CoA; via carbonyl oxygen"
/evidence="ECO:0000256|PROSITE-ProRule:PRU01065"
BINDING 1512
/note="Acetyl-CoA"
/evidence="ECO:0000256|PROSITE-ProRule:PRU01065"
BINDING 1516
/note="Acetyl-CoA"
/evidence="ECO:0000256|PROSITE-ProRule:PRU01065"
SEQUENCE 2522 AA; 274806 MW; 05B33CDC0964AFB7 CRC64;
MAENLLDGPP NPKRAKLNSP GFSASDSTDF GSLFDLENDL PDELIPNGEL GLLNSSGNLV
PDAASKHKQL SELLRGGSGS SLNPGIGNVN SNSPVQQGVG SQVQGQPNSA SIGNLGAMGK
SPLNQGDSSA SGLAKQVAST SGPTTPASQT LNSQAQKQVG MVTSSPATSQ TGPGICMNTN
FSQTHQSLLN SNSGHSLMNQ PQQGQGQVMN GSLGAAGRGR GAGMQYSAPA MQGNAGSVLA
ETLTQVSPQM AGHTGLNTAQ TGAITKMGMA GNTSPFGQPF SQTGGQQMGA TGVNPQLPNK
PGMANSLPAF PADIKSTPVT SVPNMSQMQT QVQQVGIVPT QAMATGPTAD PEKRKLIQQQ
LVLLLHAHKC QRREQANGEV RACALPHCRT MKNVLNHMTH CQAGKACQVA HCASSRQIIS
HWKNCTRHDC PVCLPLKNAS DKRNQQPLLG SPAGGMQNSI GSVGTGQQNN PSLSNPNPID
PSSMQRAYAA LGLPYGNQPQ TQLQPQVQGQ QPAQPQAHQQ MRTINALGAN QMNLPTGGIT
TDQQASLISE TALPTSLGTN NPLMNDGTNS GNVGNLSSMP TAAPPSSTGV RKAWHEHVTQ
DLRNHLVHKL VQAIFPTPDP AALKDRRMEN LVAYARKVEG DMYESANSRD EYYHLLAEKI
YKIQKELEEK RRSRLHKQGI LGTQPALQTP GPQPPGIPQV AAAMGQAQPV RPPNGPMSMT
TVPISRMQVS QGMNQFNPMS IGNVQMPQAP MGPRAASPMN HPVQMNNMGA VPAMAMSPSR
MPQPQNMMGA HSNNMMGQAP TQNQFLPQNQ FPASTGAMNV NNVGMGQSAA QAGVAQQGQV
PSAALPNSMN MLGPQSGQLC PPVTQPPLHQ TTPPVSTAAG MPPIQHQTPT GMTPPQPAAP
TQPSTPVSSS GQTPTPTPGS VPNATQTQST PTGQTAAQAQ VTPQPQTPVQ PQSVPTPQPS
QQQPTSVQAQ PPGTPLSQAA ASIDNRVPTP ASVASADTNS QQLGPDAPML ESKSEVKTEE
TEPETSETQV EAKTEVEEDL QGSSQTKEET DGTELKQEPM EIEEKKPEIK VDAKEEEESG
TNGTTSQSTS PSQPRKKIFK PEELRQALMP TLEALYRQDP ESLPFRQPVD PQLLGIPDYF
DIVKNPMDLS TIKRKLDTGQ YQEPWQYVDD VWLMFNNAWL YNRKTSRVYK FCTKLAEVFE
QEIDPVMQSL GYCCGRKYEF SPQTLCCYGK QLCTIPRDAA YYSYQNRYHF CEKCFTEIQG
ENVTLGDDPS QPQTTISKDQ FEKKKNDTLD PEPFVDCKEC GRKMHQICVL HYDIIWPSGF
VCDNCLKKTG RTRKENKFSA KRLQTTRLGN HLEDRVNKFL RRQNHPEAGE VFVRVVASSD
KTVEVKPGMK SRFVDSGEMS ESFPYRTKAL FAFEEIDGVD VCFFGMHVQE YGSDCPPPNT
RRVYISYLDS IHFFRPRCLR TAVYHEILIG YLEYVKKLGY VTGHIWACPP SEGDDYIFHC
HPPDQKIPKP KRLQEWYKKM LDKAFAERII HDYKDIFKQA TEDRLTSAKE LPYFEGDFWP
NVLEESIKEL EQEEEERKKE ESTAASETTE GSQGDSKNAK KKNNKKTNKN KSSISRANKK
KPSMPNVSND LSQKLYATME KHKEVFFVIH LHAGPVINTL PPIVDPDPLL SCDLMDGRDA
FLTLARDKHW EFSSLRRSKW STLCMLVELH TQGQDRFVYT CNECKHHVET RWHCTVCEDY
DLCINCYNTK SHDHKMVKWG LGLDDESNSQ GEQQSKSPQE SRRLSIQRCI QSLVHACQCR
NANCSLPSCQ KMKRVVQHTK GCKRKTNGGC PVCKQLIALC CYHAKHCQEN KCPVPFCLNI
KHKLRQQQIQ HRLQQAQLMR RRMATMNTRN VPQQSLPSPT SATPGTPTQQ PSTPQTPQPP
PQPQPSPVSM SPAGFPNVSR TQPPTTVSTG KPANPVAAPP PPAQPPPAAV EAARQIEREA
AQQQQQQLYR VNNINNGLPP GRPGLVNPTV GSVSQMQQVG MNVPRPSPVS GPVMSNMQPG
QWQSPPMPQQ QAMQPGMARP VMPMATAQAV AGPRMPGVQQ PPRSIPPNAL QDLLRTLKSP
SSPQQQQQVL NILKSNPQLM AAFIKQRTAK YVANQPGMQP QAGIQPQPGM QQPQTGMQQP
GMHAQPGLQN MNAMQAGVQR PSVPPQQQGI GAMNPQGQAI NIMNPGHNTS MASMNHPQYR
EILRRQLLQQ QQQQQQQQGG AGMAAGMAGH SQFQQPQGPG GYPQAMQQQR MQQHISIQGG
SMGQMAQMGQ LNQMGQPGLG ADGTPNIQQA LQQRILQQQQ MKQQIGSPGQ PNPMSPQQHM
LSGQPQASHL PGQQIATSLS SQVRSPAPVQ SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT
GSPHPGLAVT MASSMDQGHL GNPEQSAMLP QLNTPNRSAL SNELSLTSRL KAEEKKNIDK
LPAGRPPRDG TAPVVGRFSI CELSEGGAGR WDGLRAHSAR SRSAGHADVE IVALFSLIKN
WF


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EIAAB09459 CREB-regulated transcription coactivator 2,Crtc2,Mouse,Mus musculus,Torc2,TORC-2,Transducer of CREB protein 2,Transducer of regulated cAMP response element-binding protein 2
EIAAB09456 Bos taurus,Bovine,CREB-regulated transcription coactivator 2,CRTC2,TORC2,TORC-2,Transducer of CREB protein 2,Transducer of regulated cAMP response element-binding protein 2
EIAAB09460 CREB-regulated transcription coactivator 3,Crtc3,Mouse,Mus musculus,Torc3,TORC-3,Transducer of CREB protein 3,Transducer of regulated cAMP response element-binding protein 3
EIAAB09461 CREB-regulated transcription coactivator 3,CRTC3,Homo sapiens,Human,TORC3,TORC-3,Transducer of CREB protein 3,Transducer of regulated cAMP response element-binding protein 3
EIAAB09457 CREB-regulated transcription coactivator 2,CRTC2,Homo sapiens,Human,TORC2,TORC-2,Transducer of CREB protein 2,Transducer of regulated cAMP response element-binding protein 2
Pathways :
WP2292: Chemokine signaling pathway
WP1616: ABC transporters
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP731: Sterol regulatory element binding protein related
WP1531: Vitamin D synthesis
WP1502: Mitochondrial biogenesis
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP163: Cytoplasmic Ribosomal Proteins
WP1049: G Protein Signaling Pathways
WP1693: Purine metabolism
WP590: Cardiovascular Signaling
WP834: Cytoplasmic Ribosomal Proteins
WP1650: Fluorobenzoate degradation
WP2039: CDKN1A-EGF-CREB
WP1659: Glycine, serine and threonine metabolism
WP2137: Prenatal Stress & BDNF
WP1834: Interactions of the immunoglobulin superfamily (IgSF) member proteins
WP1225: estrogen signalling
WP1713: Two-component system
WP712: Estrogen signaling pathway
WP1493: Carbon assimilation C4 pathway
WP1825: GPCR ligand binding
WP813: G Protein Signaling Pathways
WP1665: Limonene and pinene degradation
WP2203: TSLP Signaling Pathway

Related Genes :

Bibliography :
[32629237] N-3 PUFA improved pup separation-induced postpartum depression via serotonergic pathway regulated by miRNA.
[32619059] Jiawei Shengmai San herbal formula ameliorates diabetic associate cognitive decline by modulating AKT and CREB in rats.
[32613466] N-3 PUFA Have Antidepressant-like Effects Via Improvement of the HPA-Axis and Neurotransmission in Rats Exposed to Combined Stress.
[32605164] Influence of Intermittent Cold Stimulations on CREB and Its Targeting Genes in Muscle: Investigations into Molecular Mechanisms of Local Cryotherapy.
[32603894] Counteracting role of nuclear factor erythroid 2-related factor 2 pathway in Alzheimer's disease.
[32603820] CREB and BDNF: Neurobiology and treatment of Alzheimer's disease.
[32603375] Paradoxical activation of AMPK by glucose drives selective EP300 activity in colorectal cancer.
[32600176] Lgr4 Governs a Pro-Inflammatory Program in Macrophages to Antagonize Post-Infarction Cardiac Repair.
[32594057] Enriched environment enhances histone acetylation of NMDA receptor in the hippocampus and improves cognitive dysfunction in aged mice.
[32582541] The KDM Inhibitor GSKJ4 Triggers CREB Downregulation via a Protein Kinase A and Proteasome-Dependent Mechanism in Human Acute Myeloid Leukemia Cells.