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ATP-binding cassette sub-family A member 1 (ATP-binding cassette transporter 1) (ABC-1) (ATP-binding cassette 1)

 ABCA1_MOUSE             Reviewed;        2261 AA.
P41233; B1AWZ8;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
20-DEC-2017, entry version 171.
RecName: Full=ATP-binding cassette sub-family A member 1;
AltName: Full=ATP-binding cassette transporter 1;
Short=ABC-1;
Short=ATP-binding cassette 1;
Name=Abca1; Synonyms=Abc1;
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].
STRAIN=DBA/2J; TISSUE=Macrophage;
PubMed=8088782; DOI=10.1006/geno.1994.1237;
Luciani M.-F., Denizot F., Savary S., Mattei M.-G., Chimini G.;
"Cloning of two novel ABC transporters mapping on human chromosome
9.";
Genomics 21:150-159(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=11352567; DOI=10.1006/geno.2000.6467;
Qiu Y., Cavelier L., Chiu S., Yang X., Rubin E., Cheng J.-F.;
"Human and mouse ABCA1 comparative sequencing and transgenesis studies
revealing novel regulatory sequences.";
Genomics 73:66-76(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
INDUCTION BY LIPOPOLYSACCHARIDE.
PubMed=12032171;
Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.;
"Bacterial lipopolysaccharide induces expression of ABCA1 but not
ABCG1 via an LXR-independent pathway.";
J. Lipid Res. 43:952-959(2002).
[6]
DOWN-REGULATION BY ENDOTOXIN.
PubMed=12777468; DOI=10.1194/jlr.M300100-JLR200;
Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C.,
Feingold K.R.;
"Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and
ABCG1 in J774 murine macrophages: differential role of LXR.";
J. Lipid Res. 44:1728-1736(2003).
[7]
INTERACTION WITH MEGF10.
PubMed=17205124; DOI=10.1371/journal.pone.0000120;
Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
Zhou Z., Chimini G.;
"Cooperation between engulfment receptors: the case of ABCA1 and
MEGF10.";
PLoS ONE 1:E120-E120(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1296, 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).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-489.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1296, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
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).
-!- FUNCTION: cAMP-dependent and sulfonylurea-sensitive anion
transporter. Key gatekeeper influencing intracellular cholesterol
transport (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with MEGF10. {ECO:0000269|PubMed:17205124}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Highest
levels are found in pregnant uterus and uterus.
-!- INDUCTION: Down-regulated by endotoxins (LPS) or cytokines (TNF
and IL-1) in J774 macrophages. The down-regulation by endotoxin in
macrophages is not likely to be mediated by the liver X
receptor/retinoic X receptor (LXR/RXR).
{ECO:0000269|PubMed:12032171}.
-!- DOMAIN: Multifunctional polypeptide with two homologous halves,
each containing a hydrophobic membrane-anchoring domain and an ATP
binding cassette (ABC) domain.
-!- PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux.
{ECO:0000250}.
-!- PTM: Palmitoylation by DHHC8 is essential for membrane
localization. {ECO:0000250}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG39073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA53530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X75926; CAA53530.1; ALT_INIT; mRNA.
EMBL; AF287263; AAG39073.1; ALT_INIT; Genomic_DNA.
EMBL; AL807243; CAM18883.1; -; Genomic_DNA.
EMBL; AL772397; CAM18883.1; JOINED; Genomic_DNA.
EMBL; AL772397; CAM27437.1; -; Genomic_DNA.
EMBL; AL807243; CAM27437.1; JOINED; Genomic_DNA.
EMBL; CH466565; EDL02285.1; -; Genomic_DNA.
CCDS; CCDS18187.1; -.
PIR; A54774; A54774.
RefSeq; NP_038482.3; NM_013454.3.
UniGene; Mm.277376; -.
ProteinModelPortal; P41233; -.
SMR; P41233; -.
BioGrid; 197900; 1.
IntAct; P41233; 2.
STRING; 10090.ENSMUSP00000030010; -.
BindingDB; P41233; -.
ChEMBL; CHEMBL1641361; -.
SwissLipids; SLP:000000484; -.
TCDB; 3.A.1.211.1; the atp-binding cassette (abc) superfamily.
iPTMnet; P41233; -.
PhosphoSitePlus; P41233; -.
SwissPalm; P41233; -.
MaxQB; P41233; -.
PaxDb; P41233; -.
PeptideAtlas; P41233; -.
PRIDE; P41233; -.
Ensembl; ENSMUST00000030010; ENSMUSP00000030010; ENSMUSG00000015243.
GeneID; 11303; -.
KEGG; mmu:11303; -.
UCSC; uc008swu.1; mouse.
CTD; 19; -.
MGI; MGI:99607; Abca1.
eggNOG; KOG0059; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00760000118965; -.
HOGENOM; HOG000231547; -.
HOVERGEN; HBG050436; -.
InParanoid; P41233; -.
KO; K05641; -.
OMA; IQTISRF; -.
OrthoDB; EOG091G007E; -.
TreeFam; TF105191; -.
Reactome; R-MMU-8963896; HDL assembly.
PMAP-CutDB; B1AWZ8; -.
PRO; PR:P41233; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000015243; -.
Genevisible; P41233; MM.
GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0045335; C:phagocytic vesicle; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0008509; F:anion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0034186; F:apolipoprotein A-I binding; ISO:MGI.
GO; GO:0034188; F:apolipoprotein A-I receptor activity; ISO:MGI.
GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0016887; F:ATPase activity; ISO:MGI.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0051117; F:ATPase binding; ISO:MGI.
GO; GO:0017127; F:cholesterol transporter activity; IDA:MGI.
GO; GO:0090554; F:phosphatidylcholine-translocating ATPase activity; ISO:MGI.
GO; GO:0090556; F:phosphatidylserine-translocating ATPase activity; ISO:MGI.
GO; GO:0005548; F:phospholipid transporter activity; IDA:MGI.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0031267; F:small GTPase binding; ISO:MGI.
GO; GO:0019905; F:syntaxin binding; ISO:MGI.
GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
GO; GO:0033344; P:cholesterol efflux; IDA:MGI.
GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
GO; GO:0016197; P:endosomal transport; ISO:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:MGI.
GO; GO:0034380; P:high-density lipoprotein particle assembly; ISO:MGI.
GO; GO:0050702; P:interleukin-1 beta secretion; ISO:MGI.
GO; GO:0032367; P:intracellular cholesterol transport; ISO:MGI.
GO; GO:0042158; P:lipoprotein biosynthetic process; IMP:MGI.
GO; GO:0042157; P:lipoprotein metabolic process; IMP:MGI.
GO; GO:0007040; P:lysosome organization; ISO:MGI.
GO; GO:0002790; P:peptide secretion; IMP:MGI.
GO; GO:0006911; P:phagocytosis, engulfment; IMP:MGI.
GO; GO:0033700; P:phospholipid efflux; IDA:MGI.
GO; GO:0055091; P:phospholipid homeostasis; ISO:MGI.
GO; GO:0045332; P:phospholipid translocation; IMP:MGI.
GO; GO:0060155; P:platelet dense granule organization; ISO:MGI.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; ISO:MGI.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
GO; GO:0006497; P:protein lipidation; IMP:MGI.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:MGI.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
GO; GO:0055098; P:response to low-density lipoprotein particle stimulus; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR026082; ABCA.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR19229; PTHR19229; 1.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Complete proteome; Disulfide bond; Glycoprotein;
Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 2261 ATP-binding cassette sub-family A member
1.
/FTId=PRO_0000093289.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 639 Extracellular. {ECO:0000250}.
TRANSMEM 640 660 Helical. {ECO:0000255}.
TRANSMEM 683 703 Helical. {ECO:0000255}.
TRANSMEM 716 736 Helical. {ECO:0000255}.
TRANSMEM 745 765 Helical. {ECO:0000255}.
TRANSMEM 777 797 Helical. {ECO:0000255}.
TRANSMEM 827 847 Helical. {ECO:0000255}.
TRANSMEM 941 961 Helical. {ECO:0000255}.
TRANSMEM 1351 1371 Helical. {ECO:0000255}.
TOPO_DOM 1372 1656 Extracellular. {ECO:0000250}.
TRANSMEM 1657 1677 Helical. {ECO:0000255}.
TRANSMEM 1703 1723 Helical. {ECO:0000255}.
TRANSMEM 1735 1755 Helical. {ECO:0000255}.
TRANSMEM 1768 1788 Helical. {ECO:0000255}.
TRANSMEM 1802 1822 Helical. {ECO:0000255}.
TRANSMEM 1852 1872 Helical. {ECO:0000255}.
DOMAIN 899 1131 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 1912 2144 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 933 940 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1946 1953 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 1042 1042 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:O95477}.
MOD_RES 1296 1296 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 2054 2054 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:O95477}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 23 23 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 1110 1110 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 1111 1111 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 14 14 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 489 489 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 521 521 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 820 820 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1144 1144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1294 1294 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1453 1453 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1499 1499 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1504 1504 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1637 1637 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2044 2044 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2238 2238 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 75 309 {ECO:0000250}.
DISULFID 1463 1477 {ECO:0000250}.
CONFLICT 1567 1568 Missing (in Ref. 2; AAG39073).
{ECO:0000305}.
CONFLICT 1568 1568 S -> T (in Ref. 1; CAA53530).
{ECO:0000305}.
CONFLICT 2024 2024 V -> F (in Ref. 1; CAA53530).
{ECO:0000305}.
CONFLICT 2024 2024 Missing (in Ref. 2; AAG39073).
{ECO:0000305}.
SEQUENCE 2261 AA; 253912 MW; E041DA4FA73C2660 CRC64;
MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE QHECHFPNKA
MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS IVSRLFSDAQ RLLLYSQRDT
SIKDMHKVLR MLRQIKHPNS NLKLQDFLVD NETFSGFLQH NLSLPRSTVD SLLQANVGLQ
KVFLQGYQLH LASLCNGSKL EEIIQLGDAE VSALCGLPRK KLDAAERVLR YNMDILKPVV
TKLNSTSHLP TQHLAEATTV LLDSLGGLAQ ELFSTKSWSD MRQEVMFLTN VNSSSSSTQI
YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNNTE EDVDTFYDNS TTPYCNDLMK
NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN KTFQELAVFH DLEGMWEELS
PQIWTFMENS QEMDLVRTLL DSRGNDQFWE QKLDGLDWTA QDIMAFLAKN PEDVQSPNGS
VYTWREAFNE TNQAIQTISR FMECVNLNKL EPIPTEVRLI NKSMELLDER KFWAGIVFTG
ITPDSVELPH HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV
EQAIIRVLTG SEKKTGVYVQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY SVAVIIKSIV
YEKEARLKET MRIMGLDNGI LWFSWFVSSL IPLLVSAGLL VVILKLGNLL PYSDPSVVFV
FLSVFAMVTI LQCFLISTLF SRANLAAACG GIIYFTLYLP YVLCVAWQDY VGFSIKIFAS
LLSPVAFGFG CEYFALFEEQ GIGVQWDNLF ESPVEEDGFN LTTAVSMMLF DTFLYGVMTW
YIEAVFPGQY GIPRPWYFPC TKSYWFGEEI DEKSHPGSSQ KGVSEICMEE EPTHLRLGVS
IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF PPTSGTAYIL
GKDIRSEMSS IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL KGLSEKHVKA EMEQMALDVG
LPPSKLKSKT SQLSGGMQRK LSVALAFVGG SKVVILDEPT AGVDPYSRRG IWELLLKYRQ
GRTIILSTHH MDEADILGDR IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS
SCRNSSSTVS CLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI
GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK VAEESGVDAE
TSDGTLPARR NRRAFGDKQS CLHPFTEDDA VDPNDSDIDP ESRETDLLSG MDGKGSYQLK
GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ
PWMYNEQYTF VSNDAPEDMG TQELLNALTK DPGFGTRCME GNPIPDTPCL AGEEDWTISP
VPQSIVDLFQ NGNWTMKNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QKTADILQNL
TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NSQALPPSHE VNDAIKQMKK
LLKLTKDSSA DRFLSSLGRF MAGLDTKNNV KVWFNNKGWH AISSFLNVIN NAILRANLQK
GENPSQYGIT AFNHPLNLTK QQLSEVALMT TSVDVLVSIC VIFAMSFVPA SFVVFLIQER
VSKAKHLQFI SGVKPVIYWL SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL
LLLLYGWSIT PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTNNKLNDIN
DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG RNLFAMAVEG
VVFFLITVLI QYRFFIRPRP VKAKLPPLND EDEDVRRERQ RILDGGGQND ILEIKELTKI
YRRKRKPAVD RICIGIPPGE CFGLLGVNGA GKSTTFKMLT GDTPVTRGDA FLNKNSILSN
IHEVHQNMGY CPQFDAITEL LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK
YASNYSGGNK RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSI VKEGRSVVLT
SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP DLKPVQEFFG
LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR LHIEDYSVSQ TTLDQVFVNF
AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF LQDEKVKESY V


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U1181m CLIA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Kiaa1520,mABCB9,Mouse,Mus musculus,TAPL,TAP-like protein 96T
E1181m ELISA kit ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Kiaa1520,mABCB9,Mouse,Mus musculus,TAPL,TAP-like protein 96T
E1181r ELISA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Rat,Rattus norvegicus,TAPL,TAP-like protein 96T
E1181r ELISA kit ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Rat,Rattus norvegicus,TAPL,TAP-like protein 96T
U1181r CLIA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Rat,Rattus norvegicus,TAPL,TAP-like protein 96T
20-372-60004 ATP-binding cassette - Mouse monoclonal anti-human ABCF_ antibody; ATP-binding cassette. sub-family F (GCN20). member 1. isoform CRA_a; ABC50 protein Monoclonal 0.1 mg
20-271-80098 ABCA1 - Mouse Anti ABCA1; ATP-binding cassette transporter 1; ATP-binding cassette 1; ABC-1; Cholesterol efflux regulatory protein Monoclonal 0.1 mg
GWB-9F6073 Anti- LOC342293 (similar to ATP-binding cassette transporter sub-family A member 15) Antibody
U1068r CLIA Abcc1,ATP-binding cassette sub-family C member 1,Leukotriene C(4) transporter,LTC4 transporter,Mrp1,Multidrug resistance-associated protein 1,Rat,Rattus norvegicus 96T
U1068b CLIA ABCC1,ATP-binding cassette sub-family C member 1,Bos taurus,Bovine,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
E1068r ELISA kit Abcc1,ATP-binding cassette sub-family C member 1,Leukotriene C(4) transporter,LTC4 transporter,Mrp1,Multidrug resistance-associated protein 1,Rat,Rattus norvegicus 96T
E1068b ELISA ABCC1,ATP-binding cassette sub-family C member 1,Bos taurus,Bovine,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
E1068r ELISA Abcc1,ATP-binding cassette sub-family C member 1,Leukotriene C(4) transporter,LTC4 transporter,Mrp1,Multidrug resistance-associated protein 1,Rat,Rattus norvegicus 96T
E1068b ELISA kit ABCC1,ATP-binding cassette sub-family C member 1,Bos taurus,Bovine,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
E1068h ELISA ABCC1,ATP-binding cassette sub-family C member 1,Homo sapiens,Human,Leukotriene C(4) transporter,LTC4 transporter,MRP,MRP1,Multidrug resistance-associated protein 1 96T


 

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