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Futsch, isoform F

 M9NGG5_DROME            Unreviewed;      5495 AA.
M9NGG5;
26-JUN-2013, integrated into UniProtKB/TrEMBL.
26-JUN-2013, sequence version 1.
22-NOV-2017, entry version 44.
SubName: Full=Futsch, isoform F {ECO:0000313|EMBL:AFH07176.1};
Name=futsch {ECO:0000313|EMBL:AFH07176.1,
ECO:0000313|FlyBase:FBgn0259108};
Synonyms=22C10 {ECO:0000313|EMBL:AFH07176.1},
22c10 {ECO:0000313|EMBL:AFH07176.1},
22C20 {ECO:0000313|EMBL:AFH07176.1},
CG14772 {ECO:0000313|EMBL:AFH07176.1},
CG3064 {ECO:0000313|EMBL:AFH07176.1},
Dmel\CG34387 {ECO:0000313|EMBL:AFH07176.1},
EG:49E4.1 {ECO:0000313|EMBL:AFH07176.1},
Futch {ECO:0000313|EMBL:AFH07176.1},
FUTSCH {ECO:0000313|EMBL:AFH07176.1},
Futsch {ECO:0000313|EMBL:AFH07176.1},
lincRNA.936 {ECO:0000313|EMBL:AFH07176.1},
Mab 22C10 {ECO:0000313|EMBL:AFH07176.1},
mAb 22C10 {ECO:0000313|EMBL:AFH07176.1},
mAb-22C10 {ECO:0000313|EMBL:AFH07176.1},
MAb22C10 {ECO:0000313|EMBL:AFH07176.1},
Mab22C10 {ECO:0000313|EMBL:AFH07176.1},
Mab22c10 {ECO:0000313|EMBL:AFH07176.1},
mAb22C10 {ECO:0000313|EMBL:AFH07176.1},
mAb22c10 {ECO:0000313|EMBL:AFH07176.1},
Map-1B {ECO:0000313|EMBL:AFH07176.1},
MAP-IB {ECO:0000313|EMBL:AFH07176.1},
MAP1B {ECO:0000313|EMBL:AFH07176.1},
Map1B {ECO:0000313|EMBL:AFH07176.1},
map1b {ECO:0000313|EMBL:AFH07176.1},
Olk {ECO:0000313|EMBL:AFH07176.1}, olk {ECO:0000313|EMBL:AFH07176.1},
ssC10 {ECO:0000313|EMBL:AFH07176.1};
ORFNames=CG34387 {ECO:0000313|EMBL:AFH07176.1,
ECO:0000313|FlyBase:FBgn0259108},
Dmel_CG34387 {ECO:0000313|EMBL:AFH07176.1};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000313|EMBL:AFH07176.1, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:AFH07176.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J.,
Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000313|EMBL:AFH07176.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537568;
Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
"Finishing a whole-genome shotgun: release 3 of the Drosophila
melanogaster euchromatic genome sequence.";
Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
[3] {ECO:0000313|EMBL:AFH07176.1, ECO:0000313|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000313|EMBL:AFH07176.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537573;
Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
Ashburner M., Celniker S.E.;
"The transposable elements of the Drosophila melanogaster euchromatin:
a genomics perspective.";
Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
[5] {ECO:0000313|EMBL:AFH07176.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537574;
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
Karpen G.H.;
"Heterochromatic sequences in a Drosophila whole-genome shotgun
assembly.";
Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
[6] {ECO:0000313|EMBL:AFH07176.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
Ashburner M., Anxolabehere D.;
"Combined evidence annotation of transposable elements in genome
sequences.";
PLoS Comput. Biol. 1:166-175(2005).
[7] {ECO:0000313|EMBL:AFH07176.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569856; DOI=10.1126/science.1139815;
Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
"The Release 5.1 annotation of Drosophila melanogaster
heterochromatin.";
Science 316:1586-1591(2007).
[8] {ECO:0000313|EMBL:AFH07176.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569867; DOI=10.1126/science.1139816;
Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
Dimitri P., Karpen G.H., Celniker S.E.;
"Sequence finishing and mapping of Drosophila melanogaster
heterochromatin.";
Science 316:1625-1628(2007).
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EMBL; AE014298; AFH07176.1; -; Genomic_DNA.
RefSeq; NP_001096864.1; NM_001103394.3.
RefSeq; NP_001162632.2; NM_001169161.3.
RefSeq; NP_001245461.1; NM_001258532.1.
UniGene; Dm.6254; -.
ProteinModelPortal; M9NGG5; -.
SMR; M9NGG5; -.
PaxDb; M9NGG5; -.
PRIDE; M9NGG5; -.
EnsemblMetazoa; FBtr0112628; FBpp0111540; FBgn0259108.
EnsemblMetazoa; FBtr0307597; FBpp0300235; FBgn0259108.
EnsemblMetazoa; FBtr0307598; FBpp0300236; FBgn0259108.
GeneID; 5740544; -.
KEGG; dme:Dmel_CG34387; -.
CTD; 5740544; -.
FlyBase; FBgn0259108; futsch.
eggNOG; KOG3592; Eukaryota.
eggNOG; ENOG410XRYM; LUCA.
OMA; MKMTFEA; -.
OrthoDB; EOG091G12OH; -.
PhylomeDB; M9NGG5; -.
ChiTaRS; futsch; fly.
GenomeRNAi; 5740544; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0259108; -.
ExpressionAtlas; M9NGG5; differential.
GO; GO:0005874; C:microtubule; IEA:InterPro.
GO; GO:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR026074; MAP1.
InterPro; IPR009603; MAP_Futsch.
InterPro; IPR036866; Metallo-hydrolase/OxRdtase.
PANTHER; PTHR13843; PTHR13843; 8.
Pfam; PF06740; DUF1213; 51.
1: Evidence at protein level;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Proteomics identification {ECO:0000213|PeptideAtlas:M9NGG5};
Reference proteome {ECO:0000313|Proteomes:UP000000803}.
COILED 955 978 {ECO:0000256|SAM:Coils}.
COILED 1046 1088 {ECO:0000256|SAM:Coils}.
COILED 4281 4308 {ECO:0000256|SAM:Coils}.
SEQUENCE 5495 AA; 592078 MW; 4CBCB11D44981FB1 CRC64;
MGDQPKATTT ATGGAAGPVP EGDAVMATTN QDALAKGAGD GPAQDAAQEP GQAEHGEPGD
GGDGGDDGAT DAGASSLPPS EIGGRAPLDT ACSDADGGAP SSLAGGIVGP PSPLTGCYLL
IVLGEPHSEE HKDNILQHLL KGFLSWDVSD CHVDLEEELN TITQHAPEGE EARHGERLIQ
YASENLVTEV LIHPQYNTLI QCMRNLLSSF TRHRHIIHAG YTFSGNGSWI LQDGTFSVAD
FSEAFQEHDV QRVIRAYADT ITMNIHCADA GLWHTLPEKA FARQCRIRIN PVDVLDTSSE
CINGFIDYLA PMVMPTSLRE LLETSDVVGN IRFTHPTLYV FPGGQGDAAL FGINGFNMLV
DGGFNRKACF WDFARHLDRL DAVLMTRLNN SNVQGLGAVV SRKRDAHVYP QIGHFFGNVP
DRKGLPSPDG DKDRDPLLID LFERGHGIVS DLKALDLKPQ CCYRNQEPVN LYHKVGHGTL
DMYVISPARD SKEVKEFLQK WHAGDQRLFA ARDSRDFNFP LQNLVSICAL LVWQPANPDD
TITRILFPGS TPDFKIQEGL EKLKHLEFMK HSTCTAKSIA PAIQTVTSTR KSLKSAIEAT
PAPPSASYKT TKFSPVASAA LAVQHPQQQD NKAKEAAAAA AAAAAAAASA ATIARAKADS
MDTDAEPEHE ADPEPADTGD EAAPTEQEPE AETEPEPEHE PEAEQDKDVG EEKKVEVLIM
KPQQATPAVI AASGKDGVDA ASADATPTGK LSKASAKGKA DKPRAEVKPV VRSRIDTKPP
KSMDRKLAKR DEKKSSPTTT PAARAPVAQN AKPKVLSRPA TKSSPSSTPA KSAKEANNRK
VLESKQQAAR VQATSTVSRR VTSTASERRV QQQAEAKTAA TGATQATQRK PISRRPRGVS
PSKRAPAPGS PVKQAKPKAA DLKKTRLDKG GTTDSSLVST PSADEATAAK KLQDLTASQE
LDAEKQRELD DLKEEQEVVR EIEAVFSRDE MKRQQHQQIK AELREMPAEG TGDGENEPDE
EEEYLIIEKE EVEQYTEDSI VEQESSMTKE EEIQKHQRDS QESEKKRKKS AEEEIEAAIA
KVEAAERKAR LEGASARQDE SELDVEPEQS KIKAEVQDII ATAKDIAKSR TEEQLAKPAE
EELSSPTPEE KLSKKTSDTK DDQIGAPVDV LPVNLQESLP EEKFSATIES GATTAPTLPE
DERIPLDQIK EDLVIEEKYV KEETKEAEAI VVATVQTLPE AAPLAIDTIL ASATKDAPKD
ANAEALGELP DSGERVLPMK MTFEAQQNLL RDVIKTPDEV ADLPVHEEAD LGLYEKDSQD
AGAKSISHKE ESAKEEKETD DEKENKVGEI ELGDEPNKVD ISHVLLKESV QEVAEKVVVI
ETTVEKKQEE IVEATTVITQ ENQEDLMEQV KDKEEHEQKI ESGIITEKEA KKSASTPEEK
ETSDITSDDE LPAQLADPTT VPPKSAKDRE DTGSIESPPT IEEAIEVEVQ AKQEAQKPVP
APEEAIKTEK SPLASKETSR PESATGSVKE DTEQTKSKKS PVPSRPESEA KDKKSPFASG
EASRPESVAE SVKDEAGKAE SRRESIAKTH KDESSLDKAK EQESRRESLA ESIKPESGID
EKSALASKEA SRPESVTDKS KEPSRRESIA ESLKAESTKD EKSAPPSKEA SRPGSVVESV
KDETEKSKEP SRRESIAESA KPPIEFREVS RPESVIDGIK DESAKPESRR DSPLASKEAS
RPESVLESVK DEPIKSTEKS RRESVAESFK ADSTKDEKSP LTSKDISRPE SAVENVMDAV
GSAERSQPES VTASRDVSRP ESVAESEKDD TDKPESVVES VIPASDVVEI EKGAADKEKG
VFVSLEIGKP DSPSEVISRP GPVVESVKPE SRRESSTEIV LPCHAEDSKE PSRPESKVEC
LKDESEVLKG STRRESVAES DKSSQPFKET SRPESAVGSM KDESMSKEPS RRESVKDGAA
QSRETSRPAS VAESAKDGAD DLKELSRPES TTQSKEAGSI KDEKSPLASE EASRPASVAE
SVKDEAEKSK EESRRESVAE KSPLPSKEAS RPASVAESIK DEAEKSKEES RRESVAEKSP
LPSKEASRPA SVAESIKDEA EKSKEESRRE SVAEKSPLPS KEASRPASVA ESIKDEAEKS
KEESRRESVA EKSPLPSKEA SRPASVAESI KDEAEKSKEE SRRESVAEKS PLPSKEASRP
ASVAESIKDE AEKSKEESRR ESVAEKSPLP SKEASRPASV AESIKDEAEK SKEESRRESV
AEKSPLPSKE ASRPASVAES IKDEAEKSKE ETRRESVAEK SPLPSKEASR PASVAESIKD
EAEKSKEESR RESAAEKSPL PSKEASRPAS VAESVKDEAD KSKEESRRES MAESGKAQSI
KGDQSPLKEV SRPESVAESV KDDPVKSKEP SRRESVAGSV TADSARDDQS PLESKGASRP
ESVVDSVKDE AEKQESRRES KTESVIPPKA KDDKSPKEVL QPVSMTETIR EDADQPMKPS
QAESRRESIA ESIKASSPRD EKSPLASKEA SRPGSVAESI KYDLDKPQII KDDKSTEHSR
RESLEDKSAV TSEKSVSRPL SVASDHEAAV AIEDDAKSSI SPKDKSRPGF VAETVSSPIE
EATMEFSKIE VVEKSSLALS LQGGSGGKLQ TDSSPVDVAE GDFSHAVASV STVTPTLTKP
AELAQIGAAK TVSSPLDEAL RTPSAPEHIS RADSPAECAS EEIASQDKSP QVLKESSRPA
WVAESKDDAA QLKSSVEDLR SPVASTEISR PASAGETASS PIEEAPKDFA EFEQAEKAVL
PLTIELKGNL PTLSSPVDVA HGDFPQTSTP TSSPTVASVQ PAELSKVDIE KTASSPIDEA
PKSLIGCPAE ERPESPAESA KDAAESVEKS KDASRPPSVV ESTKADSTKG DISPSPESVL
EGPKDDVEKS KESSRPPSVS ASITGDSTKD VSRPASVVES VKDEHDKAES RRESIAKVES
VIDEAGKSDS KSSSQDSQKD EKSTLASKEA SRRESVVESS KDDAEKSESR PESVIASGEP
VPRESKSPLD SKDTSRPGSM VESVTAEDEK SEQQSRRESV AESVKADTKK DGKSQEASRP
SSVDELLKDD DEKQESRRQS ITGSHKAMST MGDESPMDKA DKSKEPSRPE SVAESIKHEN
TKDEESPLGS RRDSVAESIK SDITKGEKSP LPSKEVSRPE SVVGSIKDEK AESRRESVAE
SVKPESSKDA TSAPPSKEHS RPESVLGSLK DEGDKTTSRR VSVADSIKDE KSLLVSQEAS
RPESEAESLK DAAAPSQETS RPESVTESVK DGKSPVASKE ASRPASVAEN AKDSADESKE
QRPESLPQSK AGSIKDEKSP LASKDEAEKS KEESRRESVA EQFPLVSKEV SRPASVAESV
KDEAEKSKEE SPLMSKEASR PASVAGSVKD EAEKSKEESR RESVAEKSPL PSKEASRPAS
VAESVKDEAD KSKEESRRES GAEKSPLASK EASRPASVAE SIKDEAEKSK EESRRESVAE
KSPLPSKEAS RPTSVAESVK DEAEKSKEES RRDSVAEKSP LASKEASRPA SVAESVQDEA
EKSKEESRRE SVAEKSPLAS KEASRPASVA ESIKDEAEKS KEESRRESVA EKSPLASKEA
SRPTSVAESV KDEAEKSKEE SSRDSVAEKS PLASKEASRP ASVAESVQDE AEKSKEESRR
ESVAEKSPLA SKEASRPASV AESVKDDAEK SKEESRRESV AEKSPLASKE ASRPASVAES
VKDEAEKSKE ESRRESVAEK SPLPSKEASR PTSVAESVKD EAEKSKEESR RESVAEKSSL
ASKKASRPAS VAESVKDEAE KSKEESRRES VAEKSPLASK EASRPASVAE SVKDEAEKSK
EESRRESVAE KSPLPSKEAS RPTSVAESVK DEADKSKEES RRESGAEKSP LASMEASRPT
SVAESVKDET EKSKEESRRE SVTEKSPLPS KEASRPTSVA ESVKDEAEKS KEESRRESVA
EKSPLASKES SRPASVAESI KDEAEGTKQE SRRESMPESG KAESIKGDQS SLASKETSRP
DSVVESVKDE TEKPEGSAID KSQVASRPES VAVSAKDEKS PLHSRPESVA DKSPDASKEA
SRSLSVAETA SSPIEEGPRS IADLSLPLNL TGEAKGKLPT LSSPIDVAEG DFLEVKAESS
PRPAVLSKPA EFSQPDTGHT ASTPVDEASP VLEEIEVVEQ HTTSGVGATG ATAETDLLDL
TETKSETVTK QSETTLFETL TSKVESKVEV LESSVKQVEE KVQTSVKQAE TTVTDSLEQL
TKKSSEQLTE IKSVLDTNFE EVAKIVADVA KVLKSDKDIT DIIPDFDERQ LEEKLKSTAD
TEEESDKSTR DEKSLEISVK VEIESEKSSP DQKSGPISIE EKDKIEQSEK AQLRQGILTS
SRPESVASQP ESVPSPSQSA ASHEHKEVEL SESHKAEKSS RPESVASQVS EKDMKTSRPA
SSTSQFSTKE GDEETTESLL HSLTTTETVE TKQMEEKSSF ESVSTSVTKS TVLSSQSTVQ
LREESTSESL SSSLKVEDSS RRESLSSLLA EKGGIATNTS LKEDTSASAS QLEELLVQSE
ECSSESIVSE IQTSIAQKSN KEIKDARETK VTSQFTTTTS SATKDDSLKE TVAEFLATEK
IVSAKEAFST EATKSADDCL KKTTASAVSS TSASQRALFV GTDESRRESL LSQASESRLT
HSDPEDEEPA DDVDERSSVK ESRSKSIATI MMTSIYKPSE DMEPISKLVE EEHEHVEELA
QEVTSTSKTT TLLQSSEQSS TTTSSTSKTG ASRVESITLT QMDQQTSQSQ GDPADRKTPP
TAPVSPGVKA MSSTGSAGSV IGAGAGAVAA GGKCESSAAS IVSSSGPMSP KDISGKSSPG
ALTSESQSIP TPLGRESHTD TPESSPKPTS PFPRVSKDEL KSLEMQHHSQ EQMLAGAAAA
AGAECEGDIP ELHELRGLEC TTALSGSTDK IITTTITTVT KVISADGKEI VTEQKTVTTT
DSSEPDSEKV VVTTTRTTSE SERDQLLPKE VALLRGLYRA STPGSEDDED LLLGSPRSAT
SYELQHSSSG VSKRSDLDAD GDESQDDIPP QYGSEEHSTA RSILLPRTAD PMATSFYGAL
PDSFDVVMKP STEPIPIQGA PSGDSQSSES VESSSQTWAG HKFLDQADKD FQRALEEHVQ
ARGAEVMSSV TAKYSYSPSK AEEMEQIVSG TAERQRFPLS DVQRARVAES GFATVGSVAS
QQQQQEKGGE VEQAVPTTTA VTASTTATAS STGALPKDRL EEWGKPLGLP SPAPLPVEGG
ADIRTTPKKE RRLVATKTRL NNEKNLRRRS ESPNKAGKKP APVYVDLTYV PHNGNSYYAH
VDFFKRVRAR YYVFSGTEPS RQVYDALLEA KQTWEDKELE VTIIPTYDTD VLGYWVAENE
ELLAKHRIDL SPSASRCTIN LQDHETSCSA YRLEF


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E1250h ELISA kit Homo sapiens,Human,Lamina-associated polypeptide 2, isoform alpha,LAP2,Thymopoietin isoform alpha,Thymopoietin-related peptide isoform alpha,TMPO,TP alpha,TPRP isoform alpha 96T
U1250h CLIA Homo sapiens,Human,Lamina-associated polypeptide 2, isoform alpha,LAP2,Thymopoietin isoform alpha,Thymopoietin-related peptide isoform alpha,TMPO,TP alpha,TPRP isoform alpha 96T
E1250h ELISA Homo sapiens,Human,Lamina-associated polypeptide 2, isoform alpha,LAP2,Thymopoietin isoform alpha,Thymopoietin-related peptide isoform alpha,TMPO,TP alpha,TPRP isoform alpha 96T
45-625 FOXP2 Antibody. This antibody is expected to recognize isoform I (NP_055306.1), isoform II (NP_683696.1) and isoform III (NP_683697.1 and NP_683698.1). 0.1 mg
45-080 LAT Antibody. This antibody is expected to recognize isoform a (NP_055202.1), isoform b (NP_001014987.1 and NP_001014989.1) and isoform c (NP_001014988.1). 0.1 mg
H-9105.0500 pTH_Related Protein Splice Isoform 3 (140_173) (human) Salt Trifluoroacetate Binding _ Synonym Hypercalcemia of Malignancy Factor Splice Isoform 3 (140_173) (human), pTH_rP Splice Isoform 3 (140_17 0.5 mg
H-9105.1000 pTH_Related Protein Splice Isoform 3 (140_173) (human) Salt Trifluoroacetate Binding _ Synonym Hypercalcemia of Malignancy Factor Splice Isoform 3 (140_173) (human), pTH_rP Splice Isoform 3 (140_17 1.0 mg
H-9105.1000 pTH_Related Protein Splice Isoform 3 (140_173) (human) Salt Trifluoroacetate Binding _ Synonym Hypercalcemia of Malignancy Factor Splice Isoform 3 (140_173) (human), pTH_rP Splice Isoform 3 (140_17 1.0 mg
H-9105.0500 pTH_Related Protein Splice Isoform 3 (140_173) (human) Salt Trifluoroacetate Binding _ Synonym Hypercalcemia of Malignancy Factor Splice Isoform 3 (140_173) (human), pTH_rP Splice Isoform 3 (140_17 0.5 mg
45-911 MTMR1 Antibody. Please note this will only recognize Human isoform 1 (NP_003819.1), not isoform 2 (NP_789746). 0.1 mg
EIAAB45911 ATP6N1B,ATP6V0A2,Bos taurus,Bovine,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2,V-ATPase 116 kDa isoform a2,V-type proton ATPase 116 kDa subunit a isoform 2
'AP55093SU-N Myoglobin isoform 2 Isoform 2 antibody Ab host: Rabbit 0.2 ml
'AP09453PU-N COX IV isoform 2 (+ Isoform 1) antibody Isotype Host Goat 0.1 mg
26-516 PHF19 contains 2 PHD-type zinc fingers. It acts as a transcritpional repressor. Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter. 0.05 mg
26-517 PHF19 contains 2 PHD-type zinc fingers. It acts as a transcritpional repressor. Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter. 0.05 mg
'AP16992PU-N COX IV isoform 1 (+ isoform 2) antibody Host Goat 0.1 mg
AP16992PU-N COX IV isoform 1 (+ isoform 2) Goat antibody Ab Aff - Purified 0.1 mg
'AP09453PU-N COX IV isoform 2 (+ Isoform 1) antibody Ab host: Goat 0.1 mg
AP09453PU-N COX IV isoform 2 (+ Isoform 1) Goat antibody Ab Aff - Purified 0.1 mg
'AP16992PU-N COX IV isoform 1 (+ isoform 2) antibody Ab host: Goat 0.1 mg
29-369 RBM14 contains 2 RRM (RNA recognition motif) domains. Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, 0.05 mg
EIAAB45905 ATP6V0A1,Chicken,Gallus gallus,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1,V-ATPase 116 kDa isoform a1,V-type proton ATPase 116 kDa subunit a isoform 1
EIAAB38501 Homo sapiens,Human,Signal-regulatory protein beta-1 isoform 3,SIRPB1,SIRP-beta-1 isoform 3
45-064 GIPC1 Antibody. This antibody is expected to recognize both isoform 1 (NP_005707.1, NP_974197.1 and NP_974199.1) and isoform 2 (NP_974196.1, NP_974198.1 and NP_974223.1). 0.1 mg


 

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