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

AP complex subunit beta

 Q24253_DROME            Unreviewed;       921 AA.
Q24253;
01-NOV-1996, integrated into UniProtKB/TrEMBL.
01-NOV-1996, sequence version 1.
05-DEC-2018, entry version 174.
RecName: Full=AP complex subunit beta {ECO:0000256|PIRNR:PIRNR002291};
Name=AP-1-2beta {ECO:0000313|EMBL:AAF49013.1,
ECO:0000313|FlyBase:FBgn0010380};
Synonyms=2 {ECO:0000313|EMBL:AAF49013.1},
2beta {ECO:0000313|EMBL:AAF49013.1},
AP-1 {ECO:0000313|EMBL:AAF49013.1},
AP-1beta {ECO:0000313|EMBL:AAF49013.1},
AP-1beta1 {ECO:0000313|EMBL:AAF49013.1},
AP-2beta {ECO:0000313|EMBL:AAF49013.1},
AP-beta1 {ECO:0000313|EMBL:AAF49013.1},
AP1beta1 {ECO:0000313|EMBL:AAF49013.1},
AP2beta2 {ECO:0000313|EMBL:AAF49013.1},
apl1 {ECO:0000313|EMBL:AAF49013.1},
apl2 {ECO:0000313|EMBL:AAF49013.1},
BAD1 {ECO:0000313|EMBL:AAF49013.1}, BAP {ECO:0000313|EMBL:AAF49013.1},
Bap {ECO:0000313|EMBL:AAF49013.1, ECO:0000313|FlyBase:FBgn0010380},
bap {ECO:0000313|EMBL:AAF49013.1},
Beta-adaptin {ECO:0000313|EMBL:AAF49013.1},
beta1 {ECO:0000313|EMBL:AAF49013.1},
beta2-ada {ECO:0000313|EMBL:AAF49013.1},
cg12532 {ECO:0000313|EMBL:AAF49013.1},
Dmel\CG12532 {ECO:0000313|EMBL:AAF49013.1};
ORFNames=CG12532 {ECO:0000313|EMBL:AAF49013.1,
ECO:0000313|FlyBase:FBgn0010380},
Dmel_CG12532 {ECO:0000313|EMBL:AAF49013.1};
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:AAF49013.1, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:CAA53509.1}
NUCLEOTIDE SEQUENCE.
PubMed=8006084;
Camidge D.R., Pearse B.M.;
"Cloning of Drosophila beta-adaptin and its localization on expression
in mammalian cells.";
J. Cell Sci. 107:709-718(1994).
[2] {ECO:0000313|EMBL:AAF49013.1, 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).
[3] {ECO:0000313|EMBL:AAF49013.1, 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).
[4] {ECO:0000313|EMBL:AAF49013.1, 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).
[5] {ECO:0000313|EMBL:AAF49013.1, 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).
[6] {ECO:0000313|EMBL:AAF49013.1, 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).
[7] {ECO:0000313|EMBL:AAV36939.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Berkeley {ECO:0000313|EMBL:AAV36939.1};
Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000313|EMBL:AAF49013.1, 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).
[9] {ECO:0000313|EMBL:AAF49013.1}
NUCLEOTIDE SEQUENCE.
Berkeley Drosophila Genome Project;
Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E.,
Yu C., Rubin G.;
"Drosophila melanogaster release 4 sequence.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000313|EMBL:AAF49013.1}
NUCLEOTIDE SEQUENCE.
Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
Svirskas R., Rubin G.;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[11] {ECO:0000313|EMBL:AAF49013.1, 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).
[12] {ECO:0000313|EMBL:AAF49013.1, 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).
[13] {ECO:0000313|EMBL:AAF49013.1}
NUCLEOTIDE SEQUENCE.
PubMed=26109357; DOI=.1534/g3.115.018929;
FlyBase Consortium;
Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B.,
St Pierre S.E., Gramates L.S., Zhou P., Schroeder A.J., Falls K.,
Strelets V., Russo S.M., Gelbart W.M.;
"Gene Model Annotations for Drosophila melanogaster: Impact of High-
Throughput Data.";
G3 (Bethesda) 5:1721-1736(2015).
[14] {ECO:0000313|EMBL:AAF49013.1}
NUCLEOTIDE SEQUENCE.
PubMed=26109356; DOI=.1534/g3.115.018937;
FlyBase Consortium;
Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B.,
St Pierre S.E., Zhou P., Schroeder A.J., Falls K., Emmert D.B.,
Russo S.M., Gelbart W.M.;
"Gene Model Annotations for Drosophila melanogaster: The Rule-
Benders.";
G3 (Bethesda) 5:1737-1749(2015).
[15] {ECO:0000313|EMBL:AAF49013.1}
NUCLEOTIDE SEQUENCE.
FlyBase;
Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00556307}.
-!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
{ECO:0000256|PIRNR:PIRNR002291}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AE014298; AAF49013.1; -; Genomic_DNA.
EMBL; BT016054; AAV36939.1; -; mRNA.
EMBL; X75910; CAA53509.1; -; mRNA.
PIR; S39295; S39295.
RefSeq; NP_523415.1; NM_078691.3.
UniGene; Dm.2885; -.
DIP; DIP-20749N; -.
IntAct; Q24253; 5.
STRING; 7227.FBpp0074558; -.
EnsemblMetazoa; FBtr0074789; FBpp0074558; FBgn0010380.
GeneID; 32987; -.
KEGG; dme:Dmel_CG12532; -.
UCSC; CG12532-RA; d. melanogaster.
CTD; 32987; -.
FlyBase; FBgn0010380; AP-1-2beta.
eggNOG; KOG1061; Eukaryota.
eggNOG; COG5096; LUCA.
GeneTree; ENSGT00940000155991; -.
KO; K12392; -.
OMA; ARASMVW; -.
OrthoDB; EOG091G019U; -.
Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
ChiTaRS; kay; fly.
GenomeRNAi; 32987; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0010380; Expressed in 32 organ(s), highest expression level in embryo.
GO; GO:0030122; C:AP-2 adaptor complex; ISS:FlyBase.
GO; GO:0030119; C:AP-type membrane coat adaptor complex; IDA:FlyBase.
GO; GO:0005905; C:clathrin-coated pit; IDA:FlyBase.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0005802; C:trans-Golgi network; IDA:FlyBase.
GO; GO:0030276; F:clathrin binding; IEA:InterPro.
GO; GO:0008565; F:protein transporter activity; IC:FlyBase.
GO; GO:0048749; P:compound eye development; IMP:FlyBase.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0010508; P:positive regulation of autophagy; IMP:FlyBase.
GO; GO:0016192; P:vesicle-mediated transport; IC:FlyBase.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 2.60.40.1150; -; 1.
Gene3D; 3.30.310.10; -; 1.
InterPro; IPR026739; AP_beta.
InterPro; IPR016342; AP_complex_bsu_1_2_4.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR015151; B-adaptin_app_sub_C.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
InterPro; IPR013041; Clathrin_app_Ig-like_sf.
InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
InterPro; IPR012295; TBP_dom_sf.
PANTHER; PTHR11134; PTHR11134; 2.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF02883; Alpha_adaptinC2; 1.
Pfam; PF09066; B2-adapt-app_C; 1.
PIRSF; PIRSF002291; AP_complex_beta; 1.
SMART; SM00809; Alpha_adaptinC2; 1.
SMART; SM01020; B2-adapt-app_C; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49348; SSF49348; 1.
SUPFAM; SSF55711; SSF55711; 1.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Membrane {ECO:0000256|PIRNR:PIRNR002291,
ECO:0000256|SAAS:SAAS00101884};
Protein transport {ECO:0000256|PIRNR:PIRNR002291,
ECO:0000256|SAAS:SAAS00468902};
Proteomics identification {ECO:0000213|PeptideAtlas:Q24253};
Reference proteome {ECO:0000313|Proteomes:UP000000803};
Transport {ECO:0000256|PIRNR:PIRNR002291,
ECO:0000256|SAAS:SAAS00468902}.
DOMAIN 691 800 Alpha_adaptinC2.
{ECO:0000259|SMART:SM00809}.
DOMAIN 809 919 B2-adapt-app_C.
{ECO:0000259|SMART:SM01020}.
SEQUENCE 921 AA; 101180 MW; 1CCFE6F8939855E5 CRC64;
MTDSKYFTTT KKGEIFELKS ELNNDKKEKK KEAVKKVIAS MTVGKDVSAL FPDVVNCMQT
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNT FVKDCEDSNP LIRALAVRTM GCIRVDKITE
YLCEPLRKCL KDEDPYVRKT AAVCVAKLYD ISATMVEDQG FLDQLKDLLS DSNPMVVANA
VAALSEINEA SQSGQPLVEM NSVTINKLLT ALNECTEWGQ VFILDSLANY SPKDEREAQS
ICERITPRLA HANAAVVLSA VKVLMKLLEM LSSDSDFCAT LTKKLAPPLV TLLSSEPEVQ
YVALRNINLI VQKRPDILKH EMKVFFVKYN DPIYVKLEKL DIMIRLANQS NIAQVLSELK
EYATEVDVDF VRKAVRAIGR CAIKVEPSAE RCVSTLLDLI QTKVNYVVQE AIVVIKDIFR
KYPNKYESII STLCENLDTL DEPEARASMV WIIGEYAERI DNADELLDSF LEGFQDENAQ
VQLQLLTAVV KLFLKRPSDT QELVQHVLSL ATQDSDNPDL RDRGFIYWRL LSTDPAAAKE
VVLADKPLIS EETDLLEPTL LDELICHISS LASVYHKPPT AFVEGRGAGV RKSLPNRAAG
SAAGAEQAEN AAGSEAMVIP NQESLIGDLL SMDINAPAMP SAPAATSNVD LLGGGLDILL
GGPPAEAAPG GATSLLGDIF GLGGATLSVG VQIPKVTWLP AEKGKGLEIQ GTFSRRNGEV
FMDMTLTNKA MQPMTNFAIQ LNKNSFGLVP ASPMQAAPLP PNQSIEVSMA LGTNGPIQRM
EPLNNLQVAV KNNIDIFYFA CLVHGNVLFA EDGQLDKRVF LNTWKEIPAA NELQYTLSGV
IGTTDGIASK MTTNNIFTIA KRNVEGQDML YQSLKLTNNI WVLLELKLQP GNPEATLSLK
SRSVEVANII FAAYEAIIRS P


Related products :

Catalog number Product name Quantity
15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.05 mg
15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.1 mg
EIAAB32876 11S regulator complex subunit beta,Activator of multicatalytic protease subunit 2,Homo sapiens,Human,PA28b,PA28beta,Proteasome activator 28 subunit beta,Proteasome activator complex subunit 2,PSME2,RE
EIAAB32875 11S regulator complex subunit beta,Activator of multicatalytic protease subunit 2,Mouse,Mus musculus,PA28b,Pa28b1,PA28beta,Proteasome activator 28 subunit beta,Proteasome activator complex subunit 2,P
EIAAB32873 11S regulator complex subunit beta,Activator of multicatalytic protease subunit 2,PA28b,PA28beta,Proteasome activator 28 subunit beta,Proteasome activator complex subunit 2,Psme2,Rat,Rattus norvegicus
20-272-190455 beta 1 + 2 Adaptin - Mouse monoclonal [100 _ 1] to beta 1 + 2 Adaptin; Adapter-related protein complex 1 beta-1 subunit; Beta-adaptin 1; Adaptor protein complex AP-1 beta-1 subunit; Golgi adaptor HA1_ 0.1 ml
EIAAB32777 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,Psmb8,Rat,Rattus norvegicus
EIAAB39001 Homo sapiens,Human,Proximal sequence element-binding transcription factor subunit beta,PSE-binding factor subunit beta,PTF subunit beta,Small nuclear RNA-activating complex polypeptide 3,SNAP50,SNAPc
EIAAB32773 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Pig,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,PSMB8,Sus scrofa
EIAAB33312 Complex III subunit 8,Complex III subunit VIII,Cytochrome b-c1 complex subunit 8,Low molecular mass ubiquinone-binding protein,Qpc,Rat,Rattus norvegicus,Ubiquinol-cytochrome c reductase complex 9.5 kD
EIAAB33299 Complex III subunit 10,Complex III subunit XI,Cytochrome b-c1 complex subunit 10,Homo sapiens,Human,Ubiquinol-cytochrome c reductase complex 6.4 kDa protein,UQCR,UQCR11
EIAAB33310 Complex III subunit 7,Complex III subunit VII,Cytochrome b-c1 complex subunit 7,Homo sapiens,Human,QP-C,Ubiquinol-cytochrome c reductase complex 14 kDa protein,UQBP,UQCRB
EIAAB08152 CAPH2,Chromosome-associated protein H2,Condensin-2 complex subunit H2,hCAP-H2,Homo sapiens,Human,Kleisin-beta,NCAPH2,Non-SMC condensin II complex subunit H2
EIAAB33300 Bos taurus,Bovine,Complex III subunit 10,Complex III subunit XI,Cytochrome b-c1 complex subunit 10,Ubiquinol-cytochrome c reductase complex 6.4 kDa protein,UQCR,UQCR11
EIAAB33298 Complex III subunit 10,Complex III subunit XI,Cytochrome b-c1 complex subunit 10,Mouse,Mus musculus,Ubiquinol-cytochrome c reductase complex 6.4 kDa protein,Uqcr,Uqcr11
EIAAB08154 Condensin-2 complex subunit H2,D15Ertd785e,Kleisin-beta,Mouse,Mus musculus,Ncaph2,Non-SMC condensin II complex subunit H2
EIAAB10234 COB,Complex III subunit 3,Complex III subunit III,CYTB,Cytochrome b,Cytochrome b-c1 complex subunit 3,Homo sapiens,Human,MTCYB,MT-CYB,Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
EIAAB33311 Bos taurus,Bovine,Complex III subunit 7,Complex III subunit VII,Cytochrome b-c1 complex subunit 7,QP-C,Ubiquinol-cytochrome c reductase complex 14 kDa protein,UQCRB
EIAAB33309 Complex III subunit 7,Complex III subunit VII,Cytochrome b-c1 complex subunit 7,Mouse,Mus musculus,Ubiquinol-cytochrome c reductase complex 14 kDa protein,Uqcrb
EIAAB32739 Lmp10,Low molecular mass protein 10,Macropain subunit MECl-1,Mecl1,Multicatalytic endopeptidase complex subunit MECl-1,Proteasome MECl-1,Proteasome subunit beta type-10,Proteasome subunit beta-2i,Psmb
E0291h ELISA C1orf193,C1orf60,Homo sapiens,Human,Int3,Integrator complex subunit 3,INTS3,Sensor of single-strand DNA complex subunit A,Sensor of ssDNA subunit A,SOSS complex subunit A,SOSS-A 96T
U0291h CLIA C1orf193,C1orf60,Homo sapiens,Human,Int3,Integrator complex subunit 3,INTS3,Sensor of single-strand DNA complex subunit A,Sensor of ssDNA subunit A,SOSS complex subunit A,SOSS-A 96T
E0291h ELISA kit C1orf193,C1orf60,Homo sapiens,Human,Int3,Integrator complex subunit 3,INTS3,Sensor of single-strand DNA complex subunit A,Sensor of ssDNA subunit A,SOSS complex subunit A,SOSS-A 96T
EIAAB10238 Bos taurus,Bovine,COB,Complex III subunit 3,Complex III subunit III,CYTB,Cytochrome b,Cytochrome b-c1 complex subunit 3,MTCYB,MT-CYB,Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
E0291m ELISA Int3,Integrator complex subunit 3,Ints3,Mouse,Mus musculus,Sensor of single-strand DNA complex subunit A,Sensor of ssDNA subunit A,SOSS complex subunit A,SOSS-A 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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | 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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | 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 | 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 | 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 | Gentaur