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

Phospholipid-transporting ATPase IC (EC 3.6.3.1) (ATPase class I type 8B member 1) (P4-ATPase flippase complex alpha subunit ATP8B1)

 AT8B1_MOUSE             Reviewed;        1251 AA.
Q148W0; Q3U010; Q6R964;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
22-NOV-2017, entry version 104.
RecName: Full=Phospholipid-transporting ATPase IC;
EC=3.6.3.1;
AltName: Full=ATPase class I type 8B member 1;
AltName: Full=P4-ATPase flippase complex alpha subunit ATP8B1;
Name=Atp8b1;
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, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
STRAIN=129;
PubMed=14976163; DOI=10.1093/hmg/ddh100;
Pawlikowska L., Groen A., Eppens E.F., Kunne C., Ottenhoff R.,
Looije N., Knisely A.S., Killeen N.P., Bull L.N., Elferink R.P.J.O.,
Freimer N.B.;
"A mouse genetic model for familial cholestasis caused by ATP8B1
mutations reveals perturbed bile salt homeostasis but no impairment in
bile secretion.";
Hum. Mol. Genet. 13:881-892(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
FUNCTION, AND MUTAGENESIS OF GLY-308.
PubMed=19478059; DOI=10.1073/pnas.0807919106;
Stapelbroek J.M., Peters T.A., van Beurden D.H., Curfs J.H.,
Joosten A., Beynon A.J., van Leeuwen B.M., van der Velden L.M.,
Bull L., Oude Elferink R.P., van Zanten B.A., Klomp L.W., Houwen R.H.;
"ATP8B1 is essential for maintaining normal hearing.";
Proc. Natl. Acad. Sci. U.S.A. 106:9709-9714(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20852622; DOI=10.1038/nm.2213;
Ray N.B., Durairaj L., Chen B.B., McVerry B.J., Ryan A.J., Donahoe M.,
Waltenbaugh A.K., O'Donnell C.P., Henderson F.C., Etscheidt C.A.,
McCoy D.M., Agassandian M., Hayes-Rowan E.C., Coon T.A., Butler P.L.,
Gakhar L., Mathur S.N., Sieren J.C., Tyurina Y.Y., Kagan V.E.,
McLennan G., Mallampalli R.K.;
"Dynamic regulation of cardiolipin by the lipid pump Atp8b1 determines
the severity of lung injury in experimental pneumonia.";
Nat. Med. 16:1120-1127(2010).
[8]
FUNCTION.
PubMed=21820390; DOI=10.1053/j.gastro.2011.07.042;
Groen A., Romero M.R., Kunne C., Hoosdally S.J., Dixon P.H.,
Wooding C., Williamson C., Seppen J., Van den Oever K., Mok K.S.,
Paulusma C.C., Linton K.J., Oude Elferink R.P.;
"Complementary functions of the flippase ATP8B1 and the floppase ABCB4
in maintaining canalicular membrane integrity.";
Gastroenterology 141:1927-1937(2011).
[9]
FUNCTION.
PubMed=21475228; DOI=10.1038/nm0411-413a;
Paulusma C.C., Houwen R.H., Williamson P.L.;
"The flip side of cardiolipin import.";
Nat. Med. 17:413-413(2011).
-!- FUNCTION: Catalytic component of a P4-ATPase flippase complex
which catalyzes the hydrolysis of ATP coupled to the transport of
aminophospholipids from the outer to the inner leaflet of various
membranes and ensures the maintenance of asymmetric distribution
of phospholipids. Phospholipid translocation seems also to be
implicated in vesicle formation and in uptake of lipid signaling
molecules. May play a role in asymmetric distribution of
phospholipids in the canicular membrane. Plays a role in bile salt
homeostasis. In cooperation with ABCB4 may be involved in
establishing integrity of the canalicular membrane thus protecting
hepatocytes from bile salts. Involved in the microvillus formation
in polarized epithelial cells; the function seems to be
independent from its flippase activity. Required for the
preservation of cochlear hair cells in the inner ear. Required for
the preservation of cochlear hair cells in the inner ear.
According PubMed:20852622 is proposed to act as cardiolipin
transporter during inflammatory injury; the function is questioned
by PubMed:21475228. {ECO:0000269|PubMed:14976163,
ECO:0000269|PubMed:19478059, ECO:0000269|PubMed:20852622,
ECO:0000269|PubMed:21475228, ECO:0000269|PubMed:21820390}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
phosphate + phospholipid(Side 2).
-!- SUBUNIT: Component of a P4-ATPase flippase complex which consists
of a catalytic alpha subunit and an accessory beta subunit. The
probable flippase ATP8B1:TMEM30A complex can form an intermediate
phosphoenzyme in vitro. Also interacts with beta subunit TMEM30B
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20852622};
Multi-pass membrane protein {ECO:0000269|PubMed:20852622}. Apical
cell membrane {ECO:0000250|UniProtKB:O43520}. Cell projection,
stereocilium {ECO:0000269|PubMed:20852622}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:O43520}. Golgi apparatus
{ECO:0000250|UniProtKB:O43520}. Note=Exit from the endoplasmic
reticulum requires the presence of TMEM30A or TMEM30B. Localizes
to apical membranes in epithelial cells.
{ECO:0000250|UniProtKB:O43520}.
-!- TISSUE SPECIFICITY: Hepatocytes, bile duct, intestinal epithelial
cells (cholangiocytes and ileocytes), and pancreatic acinar cells.
{ECO:0000269|PubMed:14976163}.
-!- DISRUPTION PHENOTYPE: Mice have unimpaired bile secretion, and no
liver damage, but show mild abnormalities including depressed
weight at weaning and elevated serum bile salt levels. Do not
suffer from jaundice or diarrhea and have normal serum bilirubin
levels and normal liver enzyme activities, except for mildly
elevated serum AST (aspartate aminotransferase) activity. Display
unimpaired transhepatic bile salt transport and are resistant to
bile salt-induced cholestasis. Upon bile salt feeding, demonstrate
serum bile salt accumulation, hepatic injury and expansion of the
systemic bile salt pool and this failure of bile salt homeostasis
occurs in the absence of any defect in hepatic bile secretion.
{ECO:0000269|PubMed:14976163}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IV subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY506548; AAR90342.1; -; mRNA.
EMBL; AK157316; BAE34046.1; -; mRNA.
EMBL; BC117946; AAI17947.1; -; mRNA.
CCDS; CCDS29304.1; -.
RefSeq; NP_001001488.2; NM_001001488.3.
UniGene; Mm.270043; -.
UniGene; Mm.456199; -.
ProteinModelPortal; Q148W0; -.
STRING; 10090.ENSMUSP00000025482; -.
iPTMnet; Q148W0; -.
PhosphoSitePlus; Q148W0; -.
MaxQB; Q148W0; -.
PaxDb; Q148W0; -.
PeptideAtlas; Q148W0; -.
PRIDE; Q148W0; -.
Ensembl; ENSMUST00000025482; ENSMUSP00000025482; ENSMUSG00000039529.
GeneID; 54670; -.
KEGG; mmu:54670; -.
UCSC; uc008fem.1; mouse.
CTD; 5205; -.
MGI; MGI:1859665; Atp8b1.
eggNOG; ENOG410KDRM; Eukaryota.
eggNOG; ENOG410XPYK; LUCA.
GeneTree; ENSGT00870000136387; -.
HOGENOM; HOG000202528; -.
InParanoid; Q148W0; -.
KO; K01530; -.
OMA; ARTQNTI; -.
OrthoDB; EOG091G0139; -.
PhylomeDB; Q148W0; -.
TreeFam; TF300654; -.
BRENDA; 3.6.3.1; 3474.
Reactome; R-MMU-936837; Ion transport by P-type ATPases.
PRO; PR:Q148W0; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000039529; -.
Genevisible; Q148W0; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
GO; GO:0015247; F:aminophospholipid transporter activity; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:1901612; F:cardiolipin binding; IDA:UniProtKB.
GO; GO:0005319; F:lipid transporter activity; IMP:MGI.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IDA:BHF-UCL.
GO; GO:0015917; P:aminophospholipid transport; IDA:BHF-UCL.
GO; GO:0008206; P:bile acid metabolic process; IMP:MGI.
GO; GO:0006855; P:drug transmembrane transport; ISO:MGI.
GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
GO; GO:0060119; P:inner ear receptor cell development; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0045332; P:phospholipid translocation; ISO:MGI.
GO; GO:0032534; P:regulation of microvillus assembly; ISO:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
GO; GO:0021650; P:vestibulocochlear nerve formation; IMP:UniProtKB.
Gene3D; 3.40.1110.10; -; 2.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR030346; ATP8B1.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006539; P-type_ATPase_IV.
InterPro; IPR032631; P-type_ATPase_N.
InterPro; IPR001757; P_typ_ATPase.
InterPro; IPR032630; P_typ_ATPase_c.
PANTHER; PTHR24092; PTHR24092; 1.
PANTHER; PTHR24092:SF48; PTHR24092:SF48; 1.
Pfam; PF16212; PhoLip_ATPase_C; 1.
Pfam; PF16209; PhoLip_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 3.
SUPFAM; SSF81653; SSF81653; 2.
SUPFAM; SSF81660; SSF81660; 2.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 1.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Cell projection; Complete proteome;
Endoplasmic reticulum; Golgi apparatus; Hearing; Hydrolase;
Lipid transport; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1251 Phospholipid-transporting ATPase IC.
/FTId=PRO_0000370862.
TOPO_DOM 1 121 Cytoplasmic. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255}.
TOPO_DOM 143 144 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 145 165 Helical. {ECO:0000255}.
TOPO_DOM 166 339 Cytoplasmic. {ECO:0000255}.
TRANSMEM 340 360 Helical. {ECO:0000255}.
TOPO_DOM 361 385 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 386 406 Helical. {ECO:0000255}.
TOPO_DOM 407 952 Cytoplasmic. {ECO:0000255}.
TRANSMEM 953 973 Helical. {ECO:0000255}.
TOPO_DOM 974 982 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 983 1003 Helical. {ECO:0000255}.
TOPO_DOM 1004 1032 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1033 1053 Helical. {ECO:0000255}.
TOPO_DOM 1054 1071 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 1072 1092 Helical. {ECO:0000255}.
TOPO_DOM 1093 1094 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1095 1115 Helical. {ECO:0000255}.
TOPO_DOM 1116 1142 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 1143 1163 Helical. {ECO:0000255}.
TOPO_DOM 1164 1251 Cytoplasmic. {ECO:0000255}.
ACT_SITE 454 454 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 893 893 Magnesium. {ECO:0000250}.
METAL 897 897 Magnesium. {ECO:0000250}.
MOD_RES 1223 1223 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MUTAGEN 308 308 G->V: Markly decreased expression,
hearing loss associated with degeneration
of cochlear hair cells and spiral
ganglion cells.
{ECO:0000269|PubMed:19478059}.
CONFLICT 104 104 G -> A (in Ref. 1; AAR90342).
{ECO:0000305}.
CONFLICT 108 108 L -> I (in Ref. 1; AAR90342).
{ECO:0000305}.
CONFLICT 155 155 T -> M (in Ref. 2; BAE34046).
{ECO:0000305}.
CONFLICT 174 174 N -> S (in Ref. 1; AAR90342).
{ECO:0000305}.
CONFLICT 176 176 R -> M (in Ref. 1; AAR90342).
{ECO:0000305}.
CONFLICT 531 531 L -> P (in Ref. 2; BAE34046).
{ECO:0000305}.
CONFLICT 575 575 N -> Y (in Ref. 2; BAE34046).
{ECO:0000305}.
CONFLICT 667 667 T -> A (in Ref. 3; AAI17947).
{ECO:0000305}.
CONFLICT 671 671 N -> K (in Ref. 3; AAI17947).
{ECO:0000305}.
CONFLICT 893 893 D -> E (in Ref. 2; BAE34046).
{ECO:0000305}.
CONFLICT 1226 1226 S -> C (in Ref. 2; BAE34046).
{ECO:0000305}.
SEQUENCE 1251 AA; 143798 MW; 394920189075875D CRC64;
MSTERDSETT FDEESQPNDE VVPYSDDETE DELEDQGSTV EPEQNRVNRE AEKKRETFRK
DCTWQVKAND RKFHEQPHFM NTKFFCIKES KYASNAIKTY KYNGFTFLPM NLFEQFKRAA
NFYFLILLIL QAIPQISTLA WYTTLVPLLL VLGITAIKDL VDDVARHKMD KEINNRTCEV
IKDGRFKIIK WKDIQVGDVI RLKKNDFIPA DILLLSSSEP NSLCYVETAE LDGETNLKFK
MALEITDQYL QIEDNLATFD GFIECEEPNN RLDKFTGTLF WKNQSFPLDA DKILLRGCVI
RNTDVCHGLV IFAGADTKIM KNSGKTRFKR TKIDYLMNYM VYTIFIVLIL VSAGLAIGHA
YWEAQVGNYS WYLYDGENAT PSYRGFLNFW GYIIVLNTMV PISLYVSVEV IRLGQSHFIN
WDLQMYYAEK DTPAKARTTT LNEQLGQIHY IFSDKTGTLT QNIMTFKKCC INGTIYGDHR
DASQHSHSKI ELVDFSWNTF ADGKLAFYDH YLIEQIQSGK EPEVRQFFFL LSICHTVMVD
RIDGQINYQA ASPDEGALVN AARNFGFAFL ARTQNTITVS ELGSERTYNV LAILDFNSDR
KRMSIIVRTP EGSIRLYCKG ADTVIYERLH RMNPTKQETQ DALDIFASET LRTLCLCYKE
IEEKEFTEWN NKFMAASVAS SNRDEALDKV YEEIEKDLIL LGATAIEDKL QDGVPETISK
LAKADIKIWV LTGDKKETAE NIGFACELLT EDTTICYGED INSLLHTRME NQRNRGGVSA
KFAPPVYEPF FPPGENRALI ITGSWLNEIL LEKKTKRSKI LKLKFPRTEE ERRMRSQSRR
RLEEKKEQRQ KNFVDLACEC SAVICCRVTP KQKAMVVDLV KRYKKAITLA IGDGANDVNM
IKTAHIGVGI SGQEGMQAVM SSDYSFAQFR YLQRLLLVHG RWSYIRMCKF LRYFFYKNFA
FTLVHFWYSF FNGYSAQTAY EDWFITLYNV LYSSLPVLLM GLLDQDVSDK LSLRFPGLYV
VGQRDLLFNY KRFFVSLLHG VLTSMVLFFI PLGAYLQTVG QDGEAPSDYQ SFAVTVASAL
VITVNFQIGL DTSYWTFVNA FSIFGSIALY FGIMFDFHSA GIHVLFPSAF QFTGTASNAL
RQPYIWLTII LTVAVCLLPV VAIRFLSMTI WPSESDKIQK HRKRLKAEEQ WKRRQSVFRR
GVSSRRSAYA FSHQRGYADL ISSGRSIRKK RSPLDAIIAD GTAEYRRTVE S


Related products :

Catalog number Product name Quantity
EIAAB45909 ATP6V0A2,Homo sapiens,Human,Lysosomal H(+)-transporting ATPase V0 subunit a2,TJ6,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2,V-ATPase 116 kDa isoform a2,V-type proton ATPase 116 k
EIAAB45577 ATP6V0E2,ATP6V0E2L,C7orf32,Homo sapiens,Human,Lysosomal 9 kDa H(+)-transporting ATPase V0 subunit e2,Vacuolar proton pump subunit e 2,V-ATPase subunit e 2,V-type proton ATPase subunit e 2
EIAAB45649 ATP6A1,ATP6V1A,ATP6V1A1,Homo sapiens,Human,Vacuolar ATPase isoform VA68,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,VPP2,V-type proton ATPase catalytic subunit A
G1337 Probable phospholipid-transporting ATPase IC (ATP8B1), Human, ELISA Kit 96T
G1338 Probable phospholipid-transporting ATPase IC (ATP8B1), Mouse, ELISA Kit 96T
CSB-EL002418MO Mouse Probable phospholipid-transporting ATPase IC(ATP8B1) ELISA kit 96T
CSB-EL002418HU Human Probable phospholipid-transporting ATPase IC(ATP8B1) ELISA kit 96T
EIAAB45573 ATP6H,ATP6V0E,ATP6V0E1,Homo sapiens,Human,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45629 ATP6AP1,ATP6IP1,ATP6S1,Bos taurus,Bovine,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45562 Atp6d,Atp6v0d1,Mouse,Mus musculus,P39,Physophilin,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,V-type proton ATPase subunit d 1
EIAAB45570 ATP6H,ATP6V0E,ATP6V0E1,Bos taurus,Bovine,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
CSB-EL002418HU Human Probable phospholipid-transporting ATPase IC(ATP8B1) ELISA kit SpeciesHuman 96T
CSB-EL002418MO Mouse Probable phospholipid-transporting ATPase IC(ATP8B1) ELISA kit SpeciesMouse 96T
EIAAB45652 Atp6a1,Atp6a2,Atp6v1a,Atp6v1a1,Mouse,Mus musculus,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
AT8B1_HUMAN ELISA Kit FOR Probable phospholipid-transporting ATPase IC; organism: Human; gene name: ATP8B1 96T
AT8B1_MOUSE ELISA Kit FOR Probable phospholipid-transporting ATPase IC; organism: Mouse; gene name: Atp8b1 96T
EIAAB45651 ATP6A1,ATP6V1A,ATP6V1A1,Bos taurus,Bovine,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45650 ATP6A1,ATP6V1A,ATP6V1A1,Pig,Sus scrofa,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45632 ATP6AP1,ATP6IP1,ATP6S1,Homo sapiens,Human,Protein XAP-3,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,VATPS1,V-type proton ATPase subunit S1,X
EIAAB45630 Atp6ap1,Atp6ip1,Atp6s1,C7-1 protein,Rat,Rattus norvegicus,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45631 Atp6ap1,Atp6ip1,Atp6s1,Mouse,Mus musculus,Protein C7-1,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
ATP8B3 ATP8B1 Gene ATPase, aminophospholipid transporter, class I, type 8B, member 1
ATP8B1 ATP8A1 Gene ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1
EIAAB45648 ATP6V1A,Chicken,Gallus gallus,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45563 32 kDa accessory protein,ATP6D,ATP6V0D1,Homo sapiens,Human,p39,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,VPATPD,V-type proton ATPase


 

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