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ABC transporter G family member 36 (ABC transporter ABCG.36) (AtABCG36) (Pleiotropic drug resistance protein 8) (Protein PENETRATION 3)

 AB36G_ARATH             Reviewed;        1469 AA.
Q9XIE2; Q8VXW5;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
30-AUG-2017, entry version 131.
RecName: Full=ABC transporter G family member 36;
Short=ABC transporter ABCG.36;
Short=AtABCG36;
AltName: Full=Pleiotropic drug resistance protein 8;
AltName: Full=Protein PENETRATION 3;
Name=ABCG36; Synonyms=PDR8, PEN3; OrderedLocusNames=At1g59870;
ORFNames=F23H11.19;
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;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 844-1469.
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]
IDENTIFICATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=12430018; DOI=10.1007/s00425-002-0889-z;
van den Brule S., Smart C.C.;
"The plant PDR family of ABC transporters.";
Planta 216:95-106(2002).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43 AND SER-45, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. La-0;
PubMed=14506206; DOI=10.1074/mcp.T300006-MCP200;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Large-scale analysis of in vivo phosphorylated membrane proteins by
immobilized metal ion affinity chromatography and mass spectrometry.";
Mol. Cell. Proteomics 2:1234-1243(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43 AND SER-45, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15308754; DOI=10.1105/tpc.104.023150;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Phosphoproteomics of the Arabidopsis plasma membrane and a new
phosphorylation site database.";
Plant Cell 16:2394-2405(2004).
[7]
GENE FAMILY, AND NOMENCLATURE.
PubMed=16506311; DOI=10.1016/j.febslet.2005.12.043;
Crouzet J., Trombik T., Fraysse A.S., Boutry M.;
"Organization and function of the plant pleiotropic drug resistance
ABC transporter family.";
FEBS Lett. 580:1123-1130(2006).
[8]
FUNCTION.
PubMed=16732289; DOI=10.1038/ng1806;
Consonni C., Humphry M.E., Hartmann H.A., Livaja M., Durner J.,
Westphal L., Vogel J., Lipka V., Kemmerling B., Schulze-Lefert P.,
Somerville S.C., Panstruga R.;
"Conserved requirement for a plant host cell protein in powdery mildew
pathogenesis.";
Nat. Genet. 38:716-720(2006).
[9]
FUNCTION, MUTAGENESIS OF GLY-354 AND GLY-915, DISRUPTION PHENOTYPE,
INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=16473969; DOI=10.1105/tpc.105.038372;
Stein M., Dittgen J., Sanchez-Rodriguez C., Hou B.-H., Molina A.,
Schulze-Lefert P., Lipka V., Somerville S.;
"Arabidopsis PEN3/PDR8, an ATP binding cassette transporter,
contributes to nonhost resistance to inappropriate pathogens that
enter by direct penetration.";
Plant Cell 18:731-746(2006).
[10]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION, AND
TISSUE SPECIFICITY.
PubMed=16415066; DOI=10.1093/pcp/pcj001;
Kobae Y., Sekino T., Yoshioka H., Nakagawa T., Martinoia E.,
Maeshima M.;
"Loss of AtPDR8, a plasma membrane ABC transporter of Arabidopsis
thaliana, causes hypersensitive cell death upon pathogen infection.";
Plant Cell Physiol. 47:309-318(2006).
[11]
SUBCELLULAR LOCATION.
PubMed=16618929; DOI=10.1073/pnas.0506958103;
Dunkley T.P.J., Hester S., Shadforth I.P., Runions J., Weimar T.,
Hanton S.L., Griffin J.L., Bessant C., Brandizzi F., Hawes C.,
Watson R.B., Dupree P., Lilley K.S.;
"Mapping the Arabidopsis organelle proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:6518-6523(2006).
[12]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION BY
CADMIUM AND LEAD.
PubMed=17355438; DOI=10.1111/j.1365-313X.2007.03044.x;
Kim D.-Y., Bovet L., Maeshima M., Martinoia E., Lee Y.;
"The ABC transporter AtPDR8 is a cadmium extrusion pump conferring
heavy metal resistance.";
Plant J. 50:207-218(2007).
[13]
GENE FAMILY, AND NOMENCLATURE.
PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A.,
Rea P.A., Samuels L., Schulz B., Spalding E.J., Yazaki K.,
Theodoulou F.L.;
"Plant ABC proteins - a unified nomenclature and updated inventory.";
Trends Plant Sci. 13:151-159(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19000165; DOI=10.1111/j.1365-313X.2008.03743.x;
Meyer D., Pajonk S., Micali C., O'Connell R., Schulze-Lefert P.;
"Extracellular transport and integration of plant secretory proteins
into pathogen-induced cell wall compartments.";
Plant J. 57:986-999(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[17]
FUNCTION.
PubMed=19095898; DOI=10.1126/science.1164627;
Clay N.K., Adio A.M., Denoux C., Jander G., Ausubel F.M.;
"Glucosinolate metabolites required for an Arabidopsis innate immune
response.";
Science 323:95-101(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Key factor that controls the extent of cell death in the
defense response. Necessary for both callose deposition and
glucosinolate activation in response to pathogens. Required for
limiting invasion by nonadapted powdery mildews. Confers
resistance to cadmium (Cd) and lead (Pb), probably as an efflux
pump of Cd2+ or Cd conjugates, and possibly, of chemicals that
mediate pathogen resistance. {ECO:0000269|PubMed:16415066,
ECO:0000269|PubMed:16473969, ECO:0000269|PubMed:16732289,
ECO:0000269|PubMed:17355438, ECO:0000269|PubMed:19000165,
ECO:0000269|PubMed:19095898}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16415066,
ECO:0000269|PubMed:16473969, ECO:0000269|PubMed:16618929,
ECO:0000269|PubMed:17355438, ECO:0000269|PubMed:19000165}; Multi-
pass membrane protein {ECO:0000269|PubMed:16415066,
ECO:0000269|PubMed:16473969, ECO:0000269|PubMed:16618929,
ECO:0000269|PubMed:17355438, ECO:0000269|PubMed:19000165}.
Note=Incoporated into pathogen-induced papillae and haustorial
encasement structures.
-!- TISSUE SPECIFICITY: Ubiquitous (at protein level). Higher levels
in root hairs, stomata, epidermal cells, and hydathodes.
Concentrated at the infection site of infected plants, including
papillae and haustoria. {ECO:0000269|PubMed:12430018,
ECO:0000269|PubMed:16415066, ECO:0000269|PubMed:17355438,
ECO:0000269|PubMed:19000165}.
-!- INDUCTION: Induced by cycloheximide (CHX), cold/dark treatment,
cadmium, lead, sclareol and sclareolide. Repressed by abscisic
acid (ABA). Induced by infection of avirulent and virulent
bacterial pathogens (P.syringae pv tomato with or without avrRpt2,
respectively) and fungal pathogens. {ECO:0000269|PubMed:12430018,
ECO:0000269|PubMed:16415066, ECO:0000269|PubMed:16473969,
ECO:0000269|PubMed:17355438}.
-!- DISRUPTION PHENOTYPE: Less sensitive to compatible pathogens
(P.syringae pv tomato) due to accelerated cell death and lesion
formation. {ECO:0000269|PubMed:16415066,
ECO:0000269|PubMed:16473969}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
family. PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC007258; AAD39329.1; -; Genomic_DNA.
EMBL; CP002684; AEE33632.1; -; Genomic_DNA.
EMBL; AY074515; AAL67129.1; -; mRNA.
EMBL; BK001007; DAA00876.1; -; Genomic_DNA.
PIR; H96622; H96622.
RefSeq; NP_176196.1; NM_104680.3.
UniGene; At.24243; -.
ProteinModelPortal; Q9XIE2; -.
BioGrid; 27506; 30.
STRING; 3702.AT1G59870.1; -.
TCDB; 3.A.1.205.9; the atp-binding cassette (abc) superfamily.
iPTMnet; Q9XIE2; -.
SwissPalm; Q9XIE2; -.
PaxDb; Q9XIE2; -.
PRIDE; Q9XIE2; -.
EnsemblPlants; AT1G59870.1; AT1G59870.1; AT1G59870.
GeneID; 842281; -.
Gramene; AT1G59870.1; AT1G59870.1; AT1G59870.
KEGG; ath:AT1G59870; -.
Araport; AT1G59870; -.
TAIR; locus:2025931; AT1G59870.
eggNOG; KOG0065; Eukaryota.
eggNOG; COG0842; LUCA.
HOGENOM; HOG000238051; -.
InParanoid; Q9XIE2; -.
OMA; SILYNAL; -.
OrthoDB; EOG09360089; -.
PhylomeDB; Q9XIE2; -.
PRO; PR:Q9XIE2; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; Q9XIE2; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IDA:TAIR.
GO; GO:0015691; P:cadmium ion transport; IMP:TAIR.
GO; GO:0071366; P:cellular response to indolebutyric acid stimulus; IMP:TAIR.
GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0009817; P:defense response to fungus, incompatible interaction; IMP:TAIR.
GO; GO:0006855; P:drug transmembrane transport; ISS:TAIR.
GO; GO:0042344; P:indole glucosinolate catabolic process; IMP:TAIR.
GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
GO; GO:0009627; P:systemic acquired resistance; IMP:TAIR.
CDD; cd03233; ABCG_PDR_domain1; 1.
CDD; cd03232; ABCG_PDR_domain2; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR013525; ABC_2_trans.
InterPro; IPR029481; ABC_trans_N.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR034001; ABCG_PDR_1.
InterPro; IPR034003; ABCG_PDR_2.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR013581; PDR_assoc.
Pfam; PF01061; ABC2_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
Pfam; PF14510; ABC_trans_N; 1.
Pfam; PF08370; PDR_assoc; 1.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 3.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Acetylation; ATP-binding; Cell membrane; Complete proteome; Membrane;
Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1469 ABC transporter G family member 36.
/FTId=PRO_0000234635.
TRANSMEM 540 560 Helical. {ECO:0000255}.
TRANSMEM 575 595 Helical. {ECO:0000255}.
TRANSMEM 621 641 Helical. {ECO:0000255}.
TRANSMEM 659 679 Helical. {ECO:0000255}.
TRANSMEM 685 705 Helical. {ECO:0000255}.
TRANSMEM 713 733 Helical. {ECO:0000255}.
TRANSMEM 772 792 Helical. {ECO:0000255}.
TRANSMEM 1216 1236 Helical. {ECO:0000255}.
TRANSMEM 1239 1259 Helical. {ECO:0000255}.
TRANSMEM 1299 1319 Helical. {ECO:0000255}.
TRANSMEM 1326 1346 Helical. {ECO:0000255}.
TRANSMEM 1356 1376 Helical. {ECO:0000255}.
TRANSMEM 1384 1404 Helical. {ECO:0000255}.
TRANSMEM 1441 1461 Helical. {ECO:0000255}.
DOMAIN 171 444 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 522 735 ABC transmembrane type-2 1.
DOMAIN 867 1119 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 1192 1406 ABC transmembrane type-2 2.
NP_BIND 204 211 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 912 919 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 43 43 Phosphothreonine.
{ECO:0000244|PubMed:14506206,
ECO:0000244|PubMed:15308754}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:14506206,
ECO:0000244|PubMed:15308754}.
MUTAGEN 354 354 G->D: In pen3-1; more susceptible to
Plectosphaerella cucumerina, with higher
frequency of fungal penetration and
increased formation of elongating
secondary hyphae after the first
haustorium development.
{ECO:0000269|PubMed:16473969}.
MUTAGEN 915 915 G->S: In pen3-2; more susceptible to P.
cucumerina, with higher frequency of
fungal penetration and increased
formation of elongating secondary hyphae
after the first haustorium development.
{ECO:0000269|PubMed:16473969}.
SEQUENCE 1469 AA; 165082 MW; 54B39B2EEAAEED07 CRC64;
MDYNPNLPPL GGGGVSMRRS ISRSVSRASR NIEDIFSSGS RRTQSVNDDE EALKWAAIEK
LPTYSRLRTT LMNAVVEDDV YGNQLMSKEV DVTKLDGEDR QKFIDMVFKV AEQDNERILT
KLRNRIDRVG IKLPTVEVRY EHLTIKADCY TGNRSLPTLL NVVRNMGESA LGMIGIQFAK
KAQLTILKDI SGVIKPGRMT LLLGPPSSGK TTLLLALAGK LDKSLQVSGD ITYNGYQLDE
FVPRKTSAYI SQNDLHVGIM TVKETLDFSA RCQGVGTRYD LLNELARREK DAGIFPEADV
DLFMKASAAQ GVKNSLVTDY TLKILGLDIC KDTIVGDDMM RGISGGQKKR VTTGEMIVGP
TKTLFMDEIS TGLDSSTTFQ IVKCLQQIVH LNEATVLMSL LQPAPETFDL FDDIILVSEG
QIVYQGPRDN ILEFFESFGF KCPERKGTAD FLQEVTSKKD QEQYWVNPNR PYHYIPVSEF
ASRYKSFHVG TKMSNELAVP FDKSRGHKAA LVFDKYSVSK RELLKSCWDK EWLLMQRNAF
FYVFKTVQIV IIAAITSTLF LRTEMNTRNE GDANLYIGAL LFGMIINMFN GFAEMAMMVS
RLPVFYKQRD LLFYPSWTFS LPTFLLGIPS SILESTAWMV VTYYSIGFAP DASRFFKQFL
LVFLIQQMAA SLFRLIASVC RTMMIANTGG ALTLLLVFLL GGFLLPKGKI PDWWGWAYWV
SPLTYAFNGL VVNEMFAPRW MNKMASSNST IKLGTMVLNT WDVYHQKNWY WISVGALLCF
TALFNILFTL ALTYLNPLGK KAGLLPEEEN EDADQGKDPM RRSLSTADGN RRGEVAMGRM
SRDSAAEASG GAGNKKGMVL PFTPLAMSFD DVKYFVDMPG EMRDQGVTET RLQLLKGVTG
AFRPGVLTAL MGVSGAGKTT LMDVLAGRKT GGYIEGDVRI SGFPKVQETF ARISGYCEQT
DIHSPQVTVR ESLIFSAFLR LPKEVGKDEK MMFVDQVMEL VELDSLRDSI VGLPGVTGLS
TEQRKRLTIA VELVANPSII FMDEPTSGLD ARAAAIVMRA VRNTVDTGRT VVCTIHQPSI
DIFEAFDELM LMKRGGQVIY AGPLGQNSHK VVEYFESFPG VSKIPEKYNP ATWMLEASSL
AAELKLSVDF AELYNQSALH QRNKALVKEL SVPPAGASDL YFATQFSQNT WGQFKSCLWK
QWWTYWRSPD YNLVRFIFTL ATSLLIGTVF WQIGGNRSNA GDLTMVIGAL YAAIIFVGIN
NCSTVQPMVA VERTVFYRER AAGMYSAMPY AISQVTCELP YVLIQTVYYS LIVYAMVGFE
WKAEKFFWFV FVSYFSFLYW TYYGMMTVSL TPNQQVASIF ASAFYGIFNL FSGFFIPRPK
IPKWWIWYYW ICPVAWTVYG LIVSQYGDVE TRIQVLGGAP DLTVKQYIED HYGFQSDFMG
PVAAVLIAFT VFFAFIFAFC IRTLNFQTR


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U1068m CLIA Abcc1,Abcc1a,Abcc1b,ATP-binding cassette sub-family C member 1,Leukotriene C(4) transporter,LTC4 transporter,Mdrap,Mouse,Mrp,Multidrug resistance-associated protein 1,Mus musculus 96T
E1068m ELISA Abcc1,Abcc1a,Abcc1b,ATP-binding cassette sub-family C member 1,Leukotriene C(4) transporter,LTC4 transporter,Mdrap,Mouse,Mrp,Multidrug resistance-associated protein 1,Mus musculus 96T
EIAAB25433 ABCC4,ATP-binding cassette sub-family C member 4,Homo sapiens,Human,MOAT-B,MRP_cMOAT-related ABC transporter,MRP4,Multidrug resistance-associated protein 4,Multi-specific organic anion transporter B
U1068c CLIA ABCC1,ATP-binding cassette sub-family C member 1,Chicken,Gallus gallus,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1,RCJMB04_32d20 96T
E1068c ELISA ABCC1,ATP-binding cassette sub-family C member 1,Chicken,Gallus gallus,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1,RCJMB04_32d20 96T
E1068c ELISA kit ABCC1,ATP-binding cassette sub-family C member 1,Chicken,Gallus gallus,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1,RCJMB04_32d20 96T
U1068c CLIA ABCC1,ATP-binding cassette sub-family C member 1,Canis familiaris,Canis lupus familiaris,Dog,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
E1068c ELISA ABCC1,ATP-binding cassette sub-family C member 1,Canis familiaris,Canis lupus familiaris,Dog,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
E1068c ELISA kit ABCC1,ATP-binding cassette sub-family C member 1,Canis familiaris,Canis lupus familiaris,Dog,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
EIAAB25426 Abcc2,ATP-binding cassette sub-family C member 2,Canalicular multidrug resistance protein,Canalicular multispecific organic anion transporter 1,Cmoat,Cmrp,Mrp2,Multidrug resistance-associated protein
EIAAB25432 Abcc3,ATP-binding cassette sub-family C member 3,Canalicular multispecific organic anion transporter 2,Cmoat2,Mlp2,MLP-2,Mrp3,MRP-like protein 2,Multidrug resistance-associated protein 3,Rat,Rattus no
EIAAB25431 Abcc3,ATP-binding cassette sub-family C member 3,Canalicular multispecific organic anion transporter 2,Cmoat2,Mouse,Mrp3,Multidrug resistance-associated protein 3,Mus musculus
EIAAB36640 cAMP-inducible gene 1 protein,Ci1,Mouse,Mus musculus,Peptide transporter 3,Peptide_histidine transporter 2,Pht2,Slc15a3,Solute carrier family 15 member 3
EIAAB25434 Abcc5,Abcc5a,ATP-binding cassette sub-family C member 5,MOAT-C,Mouse,Mrp5,Multidrug resistance-associated protein 5,Multi-specific organic anion transporter C,Mus musculus,SMRP
EIAAB36707 Ergothioneine transporter,ET transporter,ETT,Homo sapiens,Human,OCTN1,Organic cation_carnitine transporter 1,SLC22A4,Solute carrier family 22 member 4,UT2H


 

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