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Karst, isoform E

 A8JNJ6_DROME            Unreviewed;      4337 AA.
A8JNJ6;
04-DEC-2007, integrated into UniProtKB/TrEMBL.
03-MAR-2009, sequence version 2.
05-JUL-2017, entry version 94.
SubName: Full=Karst, isoform E {ECO:0000313|EMBL:ABW08452.2};
Name=kst {ECO:0000313|EMBL:ABW08452.2,
ECO:0000313|FlyBase:FBgn0004167};
Synonyms=beta-Spectrin {ECO:0000313|EMBL:ABW08452.2},
beta[[H]] {ECO:0000313|EMBL:ABW08452.2},
beta[[H]]-Sp {ECO:0000313|EMBL:ABW08452.2},
beta[[H]]-SPEC {ECO:0000313|EMBL:ABW08452.2},
beta[[H]]-Spec {ECO:0000313|EMBL:ABW08452.2},
beta[[H]]-Spectrin {ECO:0000313|EMBL:ABW08452.2},
beta[[H]]spectrin {ECO:0000313|EMBL:ABW08452.2},
beta[[heavy]]-Spec {ECO:0000313|EMBL:ABW08452.2},
beta[[heavy]]-Spectrin {ECO:0000313|EMBL:ABW08452.2},
beta[[Heavy]]spectrin {ECO:0000313|EMBL:ABW08452.2},
beta[[heavy]]spectrin {ECO:0000313|EMBL:ABW08452.2},
betaH {ECO:0000313|EMBL:ABW08452.2},
betaH-Spec {ECO:0000313|EMBL:ABW08452.2},
betah-Spec {ECO:0000313|EMBL:ABW08452.2},
betaHS {ECO:0000313|EMBL:ABW08452.2},
betaHSpec {ECO:0000313|EMBL:ABW08452.2},
Dmel\CG12008 {ECO:0000313|EMBL:ABW08452.2},
Kst {ECO:0000313|EMBL:ABW08452.2},
l(3)01318 {ECO:0000313|EMBL:ABW08452.2},
Spec-beta[[H]] {ECO:0000313|EMBL:ABW08452.2};
ORFNames=CG12008 {ECO:0000313|EMBL:ABW08452.2,
ECO:0000313|FlyBase:FBgn0004167},
Dmel_CG12008 {ECO:0000313|EMBL:ABW08452.2};
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:ABW08452.2, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:ABW08452.2, 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:ABW08452.2, 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:ABW08452.2, 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:ABW08452.2, 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-RESEARCH0084(2002).
[5] {ECO:0000313|EMBL:ABW08452.2, 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:ABW08452.2, 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:ABW08452.2, 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:ABW08452.2, 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; AE014296; ABW08452.2; -; Genomic_DNA.
RefSeq; NP_001097492.2; NM_001104022.3.
UniGene; Dm.3050; -.
ProteinModelPortal; A8JNJ6; -.
SMR; A8JNJ6; -.
IntAct; A8JNJ6; 2.
STRING; 7227.FBpp0289294; -.
PaxDb; A8JNJ6; -.
PRIDE; A8JNJ6; -.
EnsemblMetazoa; FBtr0300017; FBpp0289294; FBgn0004167.
GeneID; 38418; -.
KEGG; dme:Dmel_CG12008; -.
CTD; 38418; -.
FlyBase; FBgn0004167; kst.
eggNOG; KOG0035; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00760000118813; -.
InParanoid; A8JNJ6; -.
KO; K06115; -.
OMA; QSFRKNQ; -.
OrthoDB; EOG091G002Y; -.
PhylomeDB; A8JNJ6; -.
GenomeRNAi; 38418; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0004167; -.
ExpressionAtlas; A8JNJ6; differential.
Genevisible; A8JNJ6; DM.
GO; GO:0005912; C:adherens junction; IDA:FlyBase.
GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
GO; GO:0016327; C:apicolateral plasma membrane; TAS:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0008091; C:spectrin; ISS:FlyBase.
GO; GO:0003779; F:actin binding; IDA:FlyBase.
GO; GO:0008092; F:cytoskeletal protein binding; ISS:FlyBase.
GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IMP:FlyBase.
GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IMP:FlyBase.
GO; GO:0030707; P:ovarian follicle cell development; TAS:FlyBase.
GO; GO:0007009; P:plasma membrane organization; TAS:FlyBase.
GO; GO:0010797; P:regulation of multivesicular body size involved in endosome transport; IMP:FlyBase.
GO; GO:0042060; P:wound healing; IMP:FlyBase.
GO; GO:0045186; P:zonula adherens assembly; TAS:FlyBase.
CDD; cd00014; CH; 2.
Gene3D; 1.10.418.10; -; 2.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR001715; CH-domain.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001605; PH_dom-spectrin-type.
InterPro; IPR001849; PH_domain.
InterPro; IPR001452; SH3_domain.
InterPro; IPR018159; Spectrin/alpha-actinin.
InterPro; IPR002017; Spectrin_repeat.
Pfam; PF00307; CH; 2.
Pfam; PF00435; Spectrin; 29.
PRINTS; PR00683; SPECTRINPH.
SMART; SM00033; CH; 2.
SMART; SM00233; PH; 1.
SMART; SM00326; SH3; 1.
SMART; SM00150; SPEC; 30.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Actin-binding {ECO:0000256|SAAS:SAAS00782879};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Proteomics identification {ECO:0000213|PeptideAtlas:A8JNJ6};
Reference proteome {ECO:0000313|Proteomes:UP000000803};
Repeat {ECO:0000256|SAAS:SAAS00782917};
SH3 domain {ECO:0000256|PROSITE-ProRule:PRU00192}.
DOMAIN 75 178 Actin-binding.
{ECO:0000259|PROSITE:PS50021}.
DOMAIN 196 300 Actin-binding.
{ECO:0000259|PROSITE:PS50021}.
DOMAIN 898 939 SH3. {ECO:0000259|PROSITE:PS50002}.
DOMAIN 3798 3906 PH. {ECO:0000259|PROSITE:PS50003}.
COILED 522 549 {ECO:0000256|SAM:Coils}.
COILED 997 1020 {ECO:0000256|SAM:Coils}.
COILED 2017 2044 {ECO:0000256|SAM:Coils}.
COILED 2222 2249 {ECO:0000256|SAM:Coils}.
COILED 2375 2409 {ECO:0000256|SAM:Coils}.
COILED 2546 2580 {ECO:0000256|SAM:Coils}.
COILED 3640 3690 {ECO:0000256|SAM:Coils}.
SEQUENCE 4337 AA; 497554 MW; A1CFE66B0425D34D CRC64;
MEYNSVLRSN FSRNEYRRYI SYERQSLASQ YEPGGYSALQ TPTPSNRNSA NMTQRDGIIK
FENERIKTLQ EERLHIQKKT FTKWMNSFLI KAKMEVEDLF TDLADGIKLL KLLEIISSEK
LGKPNSGRMR VHKIENVNKS LAFLHTKVRL ESIGAEDIVD GNPRLILGLI WTIILRFQIQ
EIEIDVDEEN ESSEKRSAKD ALLLWCQRKT HGYPGVNITD FTNSWRSGLG FNALIHSHRP
DLFEYSTIVN SKNSNLDNLN HAFDTAANEL GIPSLLDAED IDSARPDEKS ILTYVASYYH
TFARMKNEQK SGKRIANIVG QLMDADRKKM QYEGLTTNLL SWIRQKTLEL EQRDLPNSLE
GIQRELLAFK EYRTIEKPPK YKERSEIEAL YFTINTLLKA LNQPPYNPQD GQLVNDIEKA
WQILEYAEHH REVALRDELL RQEKLEQLNY KFEKKSVLRE GYLKEMIQVL SDPRYLRQVD
ATLKKHEAIS ADILARVERF NDLTAMAEEL DRENYHGKER VRRREQEVMA KWRQLLELLE
NQRLNLSQMS NLMNLLREIA STTEAVRELQ QQFASEDVGP HLLGVEELLQ AHSLQELQVN
TYGETLKRFN RQALPYKSSE HKDAALLAQR LADLEEAYSE LLRRSAARRA RLEEARNFHH
FMEDYDNEES WLVDKQRICK TGITAKDLRA VLSLQQKHKA LEDEIKSRKP KSGQMSTAGK
RLIGEQHPRS SEIQSRIDSL AEHWQALEAL VELRRRQLED AAEAYQFYTD ANEAESWLNE
KIALVNSRDY GNDEPSAQAL LQRHRDLQGE LNAYSGDILN LNQQADKLIK AGICTLELSA
AEPELPEVEQ EEWVNETRLV PKEVWEDEWV EKLEHKKVTE TKMLPHVKSL FPFEGQGMKM
DKGEVMLLKS KTNDDWWCVR KDNGVEGFVP ANYVREVEPR PVACIVPKAE KVKSLQKVKK
TILVRQVVPV KRIKPVSVAP KPLVQRRTST QSINENADSV EKRQQRINQT YDELQEMAQK
RHALLEDSIH LFGFYRECDD FEKWMKEKER MIKSDEGEGV DNAKRKFEKF ITDLSAASKR
VEEIDGAVDT FRRQGHSQLD KIIARQRQIH QIWQRLNNAK AQREKSLEGA SSVELFNRTC
DEAKVWMSEK MLQLDTAVIT PDLRTVQALQ RRHQNLEREL APVEDKVNRV TYLGNSVKNA
YPAEKDNVNA RQQEVQDMWQ QVQQRGSDLR NRIESEVGQQ VFNNSAKVLL AWIDSVKDQL
NADESARDVE TANNLLKKHN DLGDDIRAHD TEFVEVIQLG KQLSDGKPNM AETVAVIERL
KAEQDAIHRG WAEKQKWLLQ CVDLQMFNRE ADKIDATTKS HEAFLEYNNL GASLDEVEAI
LKRHLDFEKS LMAQDKILKG FSDNADKLIS NDHYDSKYIG DRRNQVLGKR KAVKDRAFER
KRLLQASKDF HKFAAEADDL KVWLQDKTRI AGDENYRDLS NLPRKLQKHQ AFERELRANE
GQLRNVTKDG QALVQAGNRV PEVESRVADL NKRWKDLLTL SEDKGRKLEQ AASQREHNRS
LEDAKKKVDE LDSALRSGDV GNDLRSCKDL INKQQILESE ITIWDQKVAE LVSTGDDMAH
GGHFNAQNIE AGTKELQQRF KDLRDPTQRR RAKLEESLNY HKFVFELDSE FQWINEHLPA
AKSNELGQNL HQAQSLHKKH KKLEAEIKGH QPMINKALVA GQSLISQQHP EREQVESLCQ
QLEQAWQDLE RHCGERSRKL DMSLKAQQYL FDAGEIESWL GERNNVLRST EYGRDRDSAA
KLLTKHKTIE LELDTYSGIV TEMGHSCAAM VAANHPDSKV LAAKQQLIEK MLKSLHKLAS
QRQGRLMESL YKHEYFLESD EVEQWIREQE QAASSEDYGQ DFEHLQLLQN KFDDLKHRVE
VGADRVDQCE LLAKKLIDSE SPYANEVEKR QEQLRTSWEN LLQLLNQREQ KLHAAGEIHR
FHRDVAEALF RIQDKNAALS QELGRDLNSA LALLRKHEGF ENDLVALEAQ LQVLVEDSVR
LQAKYPSNAS AIAQQQDKVV AAWNDLKERS TARGDRLAAS SDLQTFLTDV RDIVSWSSNL
RAALQAEEHV SDAAGATALK IQHDAIYGEI EAREDKFRYL NELSDSMVQT GHYAAADVEE
KCAAMLDERQ KLHAAWNKKK IMLEQKIDLF CFLRDAKQID NLSSSQQAAL SSSDFGQTVE
DVQNKIRKHD EFERLIQTQE EKVSLLQEHG RKLIEQRHYD SANIQTILQG VLARRQKVKD
LCAVRRYKLE DALLYAKFVR DCAEAKYWIN EKQKKLEADA ASYAEVTNLD EKIKKLQKHQ
AFQAEVAANQ GRIQEIQDTG VILLSKQHES SPEIKRAIEI VLEAWQGLLA ELEQRGRGLE
EAQDSLEFNS QLDKIEAWIR DKEMMVQASD TGRDLEHCNA LMRKLDDVDS DMRVDDQRVK
HINQLADKLI NQAQVPADTQ SVDKRRKDFN YNWRQLQGAL NAYRALLGGA NEIHVFNRDV
DDTADRIAEK SLAMSSTDTG RDLAAVEALI RREEALERDM SAVKQKIDQH ETAAEFLIKK
YPERGAQHIE RKLEELHKSW GNLQALSVKR QSILNEAYLA HKFVSDVKEL ELWVNDMIKK
MNNTQSPSTI NDCETQLELH QERKVEIEGR QEAFAGLKQQ GEQLSKRPQQ QQPDNVRKYL
LVLEELHQTL NEAWSERARD LTEAHQLQLF KAQVEQVEIW LANKEAFLNN DDLGDSYTAV
ERLLKKHDEF EKLLHADHVD TLQKFANSIL EGEPKDADLI REKLAYILRR KQKLLELSEE
RKQRLTQSHQ LQEFLRSLYE IDRWLVQKLQ VALDENYREP SNLQSKIQKH AAFDAELLSN
SPRVQSVIHE GERLIRGDHF AKDEIAQQVQ LLEGDWLKLK GASQTKKDKL QQAYDALAFN
RSVDEFNNWM DEVELQLSSE DYGKDLAAVS NLLKKHERLE ADVAHHGELA DQLKQKDEQF
FQAEHFLRHE IHERATVSIR RYNTLHEPLG IRRENLEDSL SLQQFLRDAE DELQWLAEKQ
LVAGSQDLGT SLLSVQGLQK KHNSLEAELT SQEPLIQALL QRGQQMIRDN HFASEQLQYK
SELLQKQLVQ LRDLAAIRRL RLLDAVESQL FYVEANEADA WMREKRPVLS SSDYGRDEVS
VQGHQKKLEV LQRELTAFKP SIEKVAKLAT GLIERNHFDS SNIAEKNAQV GQEYEDLLRL
AKERESRLGE CKKLFEYLRE TEELHEWVGD QMAVTASEDY GEDVEHVEQL ILAFESFVSN
LNANEARVEA CLERGDRLIQ ENNPYRSSIK SKRDETKQLW EELKDLVHAR QDALAGAKQV
HVYDRVADET IQLINEKDAS LISEDYGQDL ESIQALGRKH QVFESELVGI QGQVDSVLAE
AAKLGEIYPD AKEHIEVKRD ETVEAWTDLK EKTAARKNKL SQAEQLQSYF DEYRDLIAWI
NEMLAKITAP ELANSVAGAE LLLASTKDHD TEIRTRDETF AKFAANGQQL IKEKHFLAHE
VEDKIKVLQA RHELLKHTLN KRREIYELNL DTQLFLKDAE ILEQWISSRE PQLKDTKLGD
SIPQVEDLLR RHEDFEKTVA AQEEKFQAIK RITMLEQLFR HQLEQEKISK LQEKERLEKE
RLEQLKQREL QRLADERRRA EKQHEHRQNA ASQEKTPIFS SPMVTPAQTS GPQSPALSQV
QLRPPFGDDN EHLALQKSSS SGMFGDRLRR GSADANVKRA ESMKVQPKQA KRTPSFTTRR
RAQSFRKNQK GEGFDLPPVE IQGSLERKHG LQSGGKKAPV RSWKQFHTVL CGQLVCFFKD
ENDFLQQKTA TAPVNILGAK CERADDYTKK KYVFRLKLPD GSEFLFEAPS LDILNDWVRK
ISFHASLPPN MQLLSYDESM KQQSSSSPDI KVTSSVESPV SSRNSSPDSQ RRTSGAQVLD
GTATPQMAFL QRQMQQQQQQ QQSQPSSPTG GFDQKPPIPP RGAAPVASHR QSQENLVVMR
NRQSSNDLQQ SATLPAGLTG VQQNGNGKDD NALLTRNSEA RQSDNPPPLP TTMPPVGGQH
QHPQNSHSHQ NQHQAQVQQR INAFNAAASQ QHQPDYFNNN TARQQPQRIP SGRIDSTRKF
IEMEAHNNNG GTSSSPKRST INYSSSGASS NGNGNVKIGS GNSSTTTITT STTTHQVTSS
SRTVWHLTSS PTSSTKSSST GGSGEPSHAI SNPSYMGLHL NNNNDSIGIG LGGWGNTRFE
SNRPVSLQPD SISFSRVSAE SSSESEAQSI SSVSGVKGSK GTKEERRSGM FRIFGRKGDK
EKEKDKDKRR SSQVPPQ


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Catalog number Product name Quantity
46-229 Prostaglandin E Receptor 3 Antibody. This antibody is expected to recognize isoform 1 (NP_000948.2), isoform 2 (NP_942005.1), isoform 3 (NP_942006.1), isoform 4 (NP_942007.1, NP_942012.1 and NP_942013 0.1 mg
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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