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 3 (AtALA3) (EC 3.6.3.1) (Aminophospholipid ATPase 3) (Aminophospholipid flippase 3) (Protein IRREGULAR TRICHOME BRANCH 2)

 ALA3_ARATH              Reviewed;        1213 AA.
Q9XIE6; Q8RWQ3;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
28-FEB-2003, sequence version 2.
25-APR-2018, entry version 143.
RecName: Full=Phospholipid-transporting ATPase 3 {ECO:0000303|PubMed:11402198};
Short=AtALA3 {ECO:0000303|PubMed:11402198};
EC=3.6.3.1 {ECO:0000305|PubMed:11402198};
AltName: Full=Aminophospholipid ATPase 3 {ECO:0000303|PubMed:11402198};
AltName: Full=Aminophospholipid flippase 3 {ECO:0000303|PubMed:11402198};
AltName: Full=Protein IRREGULAR TRICHOME BRANCH 2 {ECO:0000303|PubMed:19566596};
Name=ALA3 {ECO:0000303|PubMed:11402198};
Synonyms=ITB2 {ECO:0000303|PubMed:19566596};
OrderedLocusNames=At1g59820 {ECO:0000312|Araport:AT1G59820};
ORFNames=F23H11.14 {ECO:0000312|EMBL:AAD39325.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11402198; DOI=10.1104/pp.126.2.696;
Axelsen K.B., Palmgren M.G.;
"Inventory of the superfamily of P-type ion pumps in Arabidopsis.";
Plant Physiol. 126:696-706(2001).
[5]
FUNCTION, MUTAGENESIS OF ASP-413, DISRUPTION PHENOTYPE, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ALIS1; ALIS3 AND
ALIS5.
PubMed=18344284; DOI=10.1105/tpc.107.054767;
Poulsen L.R., Lopez-Marques R.L., McDowell S.C., Okkeri J., Licht D.,
Schulz A., Pomorski T., Harper J.F., Palmgren M.G.;
"The Arabidopsis P4-ATPase ALA3 localizes to the Golgi and requires a
beta-subunit to function in lipid translocation and secretory vesicle
formation.";
Plant Cell 20:658-676(2008).
[6]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=19566596; DOI=10.1111/j.1365-313X.2009.03954.x;
Zhang X., Oppenheimer D.G.;
"IRREGULAR TRICHOME BRANCH 2 (ITB2) encodes a putative
aminophospholipid translocase that regulates trichome branch
elongation in Arabidopsis.";
Plant J. 60:195-206(2009).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ALIS1; ALIS3 AND
ALIS5.
PubMed=20053675; DOI=10.1091/mbc.E09-08-0656;
Lopez-Marques R.L., Poulsen L.R., Hanisch S., Meffert K.,
Buch-Pedersen M.J., Jakobsen M.K., Pomorski T.G., Palmgren M.G.;
"Intracellular targeting signals and lipid specificity determinants of
the ALA/ALIS P4-ATPase complex reside in the catalytic ALA alpha-
subunit.";
Mol. Biol. Cell 21:791-801(2010).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23667493; DOI=10.1371/journal.pone.0062577;
McDowell S.C., Lopez-Marques R.L., Poulsen L.R., Palmgren M.G.,
Harper J.F.;
"Loss of the Arabidopsis thaliana P(4)-ATPase ALA3 reduces
adaptability to temperature stresses and impairs vegetative, pollen,
and ovule development.";
PLoS ONE 8:E62577-E62577(2013).
-!- FUNCTION: Involved in transport of phospholipids. Contributes to
transmembrane flipping of lipids. Required for secretory processes
during plant development. Requires an interaction with an ALIS
protein for activity. Has activity with phosphatidylserine,
phosphatidylcholine and phosphatidylethanolamine, but not with
lysolipid (PubMed:18344284, PubMed:19566596, PubMed:20053675).
Modifies endomembranes in multiple cell types, enabling structural
changes, or signaling functions that are critical for normal
development and adaptation to varied growth environments
(PubMed:23667493). {ECO:0000269|PubMed:18344284,
ECO:0000269|PubMed:19566596, ECO:0000269|PubMed:20053675,
ECO:0000269|PubMed:23667493}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
phosphate + phospholipid(Side 2). {ECO:0000305|PubMed:11402198}.
-!- SUBUNIT: Associates with ALIS1 to form a stable and active
complex. Interacts with ALIS3 and ALIS5 in a heterologous system.
{ECO:0000269|PubMed:18344284, ECO:0000269|PubMed:20053675}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:18344284, ECO:0000269|PubMed:20053675}; Multi-
pass membrane protein {ECO:0000255}. Endoplasmic reticulum
membrane {ECO:0000269|PubMed:20053675}; Multi-pass membrane
protein {ECO:0000255}. Note=Requires the presence of an ALIS
protein to exit the endoplasmic reticulum to the Golgi.
{ECO:0000269|PubMed:20053675}.
-!- TISSUE SPECIFICITY: Expressed in petals and sepals, but not in
reproductive tissues. In siliques, detected in the upper part of
the seed pod and in the area between the seed pod and the stem,
but not in developing seeds. Strong expression in vascular shoot
tissues and in stomatal guard cells of young rosettes leaves. In
roots, expressed in cells surrounding the xylem and in central and
peripheral columella cells. Detected in developing and mature
trichomes, roots, pollen and growing pollen tubes.
{ECO:0000269|PubMed:18344284, ECO:0000269|PubMed:19566596}.
-!- DISRUPTION PHENOTYPE: Impaired growth of roots and shoots
(PubMed:18344284, PubMed:23667493). Roots devoided of the
characteristic trans-Golgi proliferation of slime vesicles
containing polysaccharides and enzymes for secretion
(PubMed:18344284). Aberrant trichome expansion, reduced primary
root growth and longer root hairs (PubMed:19566596). Impaired
pollen growth (PubMed:19566596, PubMed:23667493). Impaired ovule
development (PubMed:23667493). Reduced adaptability to temperature
stresses (PubMed:23667493). {ECO:0000269|PubMed:18344284,
ECO:0000269|PubMed:19566596, ECO:0000269|PubMed:23667493}.
-!- MISCELLANEOUS: The intracellular targeting signals and lipid
specificity determinants reside in the catalytic ALA subunit.
{ECO:0000269|PubMed:20053675}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IV subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD39325.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC007258; AAD39325.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE33621.1; -; Genomic_DNA.
EMBL; AY091777; AAM10325.1; -; mRNA.
PIR; C96622; C96622.
RefSeq; NP_176191.1; NM_104675.3.
UniGene; At.36777; -.
ProteinModelPortal; Q9XIE6; -.
BioGrid; 27500; 1.
STRING; 3702.AT1G59820.1; -.
TCDB; 3.A.3.8.6; the p-type atpase (p-atpase) superfamily.
iPTMnet; Q9XIE6; -.
PaxDb; Q9XIE6; -.
PRIDE; Q9XIE6; -.
EnsemblPlants; AT1G59820.1; AT1G59820.1; AT1G59820.
GeneID; 842275; -.
Gramene; AT1G59820.1; AT1G59820.1; AT1G59820.
KEGG; ath:AT1G59820; -.
Araport; AT1G59820; -.
TAIR; locus:2025961; AT1G59820.
eggNOG; ENOG410ITKD; Eukaryota.
eggNOG; ENOG410XPYK; LUCA.
HOGENOM; HOG000202528; -.
InParanoid; Q9XIE6; -.
KO; K14802; -.
OMA; RMRKQRG; -.
OrthoDB; EOG093600FE; -.
PhylomeDB; Q9XIE6; -.
BioCyc; ARA:AT1G59820-MONOMER; -.
BRENDA; 3.6.99.B1; 399.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-936837; Ion transport by P-type ATPases.
PRO; PR:Q9XIE6; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9XIE6; baseline and differential.
Genevisible; Q9XIE6; AT.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0005548; F:phospholipid transporter activity; IDA:TAIR.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IBA:GO_Central.
GO; GO:0048194; P:Golgi vesicle budding; IMP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0048367; P:shoot system development; IMP:TAIR.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
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.
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; Complete proteome; Endoplasmic reticulum;
Golgi apparatus; Hydrolase; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 1213 Phospholipid-transporting ATPase 3.
/FTId=PRO_0000046387.
TOPO_DOM 1 67 Cytoplasmic. {ECO:0000255}.
TRANSMEM 68 89 Helical. {ECO:0000255}.
TOPO_DOM 90 93 Extracellular. {ECO:0000255}.
TRANSMEM 94 116 Helical. {ECO:0000255}.
TOPO_DOM 117 297 Cytoplasmic. {ECO:0000255}.
TRANSMEM 298 319 Helical. {ECO:0000255}.
TOPO_DOM 320 346 Extracellular. {ECO:0000255}.
TRANSMEM 347 364 Helical. {ECO:0000255}.
TOPO_DOM 365 900 Cytoplasmic. {ECO:0000255}.
TRANSMEM 901 920 Helical. {ECO:0000255}.
TOPO_DOM 921 934 Extracellular. {ECO:0000255}.
TRANSMEM 935 954 Helical. {ECO:0000255}.
TOPO_DOM 955 984 Cytoplasmic. {ECO:0000255}.
TRANSMEM 985 1006 Helical. {ECO:0000255}.
TOPO_DOM 1007 1013 Extracellular. {ECO:0000255}.
TRANSMEM 1014 1036 Helical. {ECO:0000255}.
TOPO_DOM 1037 1042 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1043 1063 Helical. {ECO:0000255}.
TOPO_DOM 1064 1076 Extracellular. {ECO:0000255}.
TRANSMEM 1077 1087 Helical. {ECO:0000255}.
TOPO_DOM 1088 1213 Cytoplasmic. {ECO:0000255}.
ACT_SITE 413 413 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 845 845 Magnesium. {ECO:0000250}.
METAL 849 849 Magnesium. {ECO:0000250}.
MUTAGEN 413 413 D->A: Loss of internalization of
phospholipids.
{ECO:0000269|PubMed:18344284}.
SEQUENCE 1213 AA; 137753 MW; 938642DEFDA28B66 CRC64;
MVRSGSFSVD SSATHQRTPS RTVTLGHIQP QAPTYRTVYC NDRESNQPVR FKGNSISTTK
YNVFTFLPKG LFEQFRRIAN IYFLGISCLS MTPISPVSPI TNVAPLSMVL LVSLIKEAFE
DWKRFQNDMS INNSTVEILQ DQQWVSIPWR KLQVGDIVKI KKDGFFPADI LFMSSTNSDG
ICYVETANLD GETNLKIRKA LERTWDYLVP EKAYEFKGEI QCEQPNNSLY TFTGNLVVQK
QTLPLSPDQL LLRGCSLRNT EYIVGAVVFT GHETKVMMNA MNAPSKRSTL EKKLDKLIIT
IFCVLVTMCL IGAIGCSIVT DREDKYLGLH NSDWEYRNGL MIGFFTFFTL VTLFSSIIPI
SLYVSIEMIK FIQSTQFINR DLNMYHAETN TPASARTSNL NEELGQVEYI FSDKTGTLTR
NLMEFFKCSI GGVSYGCGVT EIEKGIAQRH GLKVQEEQRS TGAIREKGFN FDDPRLMRGA
WRNEPNPDLC KELFRCLAIC HTVLPEGDES PEKIVYQAAS PDEAALVTAA KNFGFFFYRR
TPTMVYVRES HVEKMGKIQD VAYEILNVLE FNSTRKRQSV VCRFPDGRLV LYCKGADNVI
FERLANGMDD VRKVTREHLE HFGSSGLRTL CLAYKDLNPE TYDSWNEKFI QAKSALRDRE
KKLDEVAELI EKDLILIGST AIEDKLQEGV PTCIETLSRA GIKIWVLTGD KMETAINIAY
ACNLINNEMK QFVISSETDA IREAEERGDQ VEIARVIKEE VKRELKKSLE EAQHSLHTVA
GPKLSLVIDG KCLMYALDPS LRVMLLSLSL NCTSVVCCRV SPLQKAQVTS LVRKGAQKIT
LSIGDGANDV SMIQAAHVGI GISGMEGMQA VMASDFAIAQ FRFLTDLLLV HGRWSYLRIC
KVVMYFFYKN LTFTLTQFWF TFRTGFSGQR FYDDWFQSLF NVVFTALPVI VLGLFEKDVS
ASLSKRYPEL YREGIRNSFF KWRVVAVWAT SAVYQSLVCY LFVTTSSFGA VNSSGKVFGL
WDVSTMVFTC LVIAVNVRIL LMSNSITRWH YITVGGSILA WLVFAFVYCG IMTPHDRNEN
VYFVIYVLMS TFYFYFTLLL VPIVSLLGDF IFQGVERWFF PYDYQIVQEI HRHESDASKA
DQLEVENELT PQEARSYAIS QLPRELSKHT GFAFDSPGYE SFFASQLGIY APQKAWDVAR
RASMRSRPKV PKK


Related products :

Catalog number Product name Quantity
ATP9A ATP8B3 Gene ATPase, aminophospholipid transporter, class I, type 8B, member 3
ATP8B3 ATP8B1 Gene ATPase, aminophospholipid transporter, class I, type 8B, member 1
ATP8B2 ATP8A2 Gene ATPase, aminophospholipid transporter, class I, type 8A, member 2
ATP8B1 ATP8A1 Gene ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1
201-20-0541 ATP8A1{ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1}rabbit.pAb 0.1ml
CSB-EL002417MO Mouse ATPase, aminophospholipid transporter-like, class I, type 8A, member 2 (ATP8A2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL002417HU Human ATPase, aminophospholipid transporter-like, class I, type 8A, member 2 (ATP8A2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL002416HU Human ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1 (ATP8A1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL002416MO Mouse ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1 (ATP8A1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-PA002416GA01HU Rabbit anti-human ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1 polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-EL002416BO Bovine ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1 (ATP8A1) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-PA002416GA01HU Rabbit anti-human ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1 polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
EIAAB34264 ATP6AP2,ATP6IP2,ATP6M8-9,ATPase H(+)-transporting lysosomal accessory protein 2,ATPase H(+)-transporting lysosomal-interacting protein 2,CAPER,ELDF10,Embryonic liver differentiation factor 10,ER-local
E1446c Rat ELISA Kit FOR Probable phospholipid-transporting ATPase IIB 96T
EIAAB34265 ATP6AP2,ATP6IP2,ATPase H(+)-transporting lysosomal accessory protein 2,ATPase H(+)-transporting lysosomal-interacting protein 2,Bos taurus,Bovine,Renin receptor,Renin_prorenin receptor,Vacuolar ATP sy
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
EIAAB34266 Atp6ap2,Atp6ip2,ATPase H(+)-transporting lysosomal accessory protein 2,ATPase H(+)-transporting lysosomal-interacting protein 2,Rat,Rattus norvegicus,Renin receptor,Renin_prorenin receptor
EIAAB34267 Atp6ap2,Atp6ip2,ATPase H(+)-transporting lysosomal accessory protein 2,ATPase H(+)-transporting lysosomal-interacting protein 2,Mouse,Mus musculus,Renin receptor,Renin_prorenin receptor
bs-1152P Peptides: ATP1b2_Na+K+ ATPase(ATPase, Na+_K+ transporting, beta 2 polypeptide) Protein Length:12-25 amino acids. 200ug lyophilized
E10871r Human ELISA Kit FOR Probable phospholipid-transporting ATPase VD 96T
E1057d Human ELISA Kit FOR Probable phospholipid-transporting ATPase IM 96T
AT11C_HUMAN Human ELISA Kit FOR Probable phospholipid-transporting ATPase IG 96T
E2000r Mouse ELISA Kit FOR Probable phospholipid-transporting ATPase IH 96T
G1338 Probable phospholipid-transporting ATPase IC (ATP8B1), Mouse, ELISA Kit 96T
G1339 Probable phospholipid-transporting ATPase ID (ATP8B2), Human, ELISA Kit 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 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