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

Respiratory burst oxidase homolog protein D (EC 1.11.1.-) (EC 1.6.3.-) (NADPH oxidase RBOHD) (AtRBOHD)

 RBOHD_ARATH             Reviewed;         921 AA.
Q9FIJ0; O81212;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
27-SEP-2017, entry version 126.
RecName: Full=Respiratory burst oxidase homolog protein D;
EC=1.11.1.-;
EC=1.6.3.-;
AltName: Full=NADPH oxidase RBOHD;
Short=AtRBOHD;
Name=RBOHD; OrderedLocusNames=At5g47910; ORFNames=MCA23.25;
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 [MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Landsberg erecta;
PubMed=9628030; DOI=10.1046/j.1365-313X.1998.00136.x;
Torres M.A., Onouchi H., Hamada S., Machida C., Hammond-Kosack K.E.,
Jones J.D.G.;
"Six Arabidopsis thaliana homologues of the human respiratory burst
oxidase (gp91phox).";
Plant J. 14:365-370(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10048488; DOI=10.1093/dnares/5.6.379;
Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. VIII.
Sequence features of the regions of 1,081,958 bp covered by seventeen
physically assigned P1 and TAC clones.";
DNA Res. 5:379-391(1998).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
FUNCTION.
PubMed=11756663; DOI=10.1073/pnas.012452499;
Torres M.A., Dangl J.L., Jones J.D.G.;
"Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for
accumulation of reactive oxygen intermediates in the plant defense
response.";
Proc. Natl. Acad. Sci. U.S.A. 99:517-522(2002).
[6]
FUNCTION, INDUCTION BY ABSCISIC ACID, AND TISSUE SPECIFICITY.
PubMed=12773379; DOI=10.1093/emboj/cdg277;
Kwak J.M., Mori I.C., Pei Z.-M., Leonhardt N., Torres M.A.,
Dangl J.L., Bloom R.E., Bodde S., Jones J.D.G., Schroeder J.I.;
"NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA
signaling in Arabidopsis.";
EMBO J. 22:2623-2633(2003).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15608336; DOI=10.1105/tpc.104.026971;
Davletova S., Rizhsky L., Liang H., Shengqiang Z., Oliver D.J.,
Coutu J., Shulaev V., Schlauch K., Mittler R.;
"Cytosolic ascorbate peroxidase 1 is a central component of the
reactive oxygen gene network of Arabidopsis.";
Plant Cell 17:268-281(2005).
[8]
FUNCTION.
PubMed=16913867; DOI=10.1111/j.1365-3040.2006.01555.x;
Kalbina I., Strid A.;
"The role of NADPH oxidase and MAP kinase phosphatase in UV-B-
dependent gene expression in Arabidopsis.";
Plant Cell Environ. 29:1783-1793(2006).
[9]
FUNCTION.
PubMed=16428598; DOI=10.1104/pp.105.073072;
Song C.J., Steinebrunner I., Wang X., Stout S.C., Roux S.J.;
"Extracellular ATP induces the accumulation of superoxide via NADPH
oxidases in Arabidopsis.";
Plant Physiol. 140:1222-1232(2006).
[10]
GENE FAMILY, AND NOMENCLATURE.
PubMed=16760484; DOI=10.1104/pp.106.078089;
Sagi M., Fluhr R.;
"Production of reactive oxygen species by plant NADPH oxidases.";
Plant Physiol. 141:336-340(2006).
[11]
FUNCTION, ENZYME REGULATION, AND INDUCTION.
PubMed=17601167; DOI=10.1094/MPMI-20-7-0794;
Fagard M., Dellagi A., Roux C., Perino C., Rigault M., Boucher V.,
Shevchik V.E., Expert D.;
"Arabidopsis thaliana expresses multiple lines of defense to
counterattack Erwinia chrysanthemi.";
Mol. Plant Microbe Interact. 20:794-805(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-343 AND SER-347,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. La-0;
PubMed=17651370; DOI=10.1111/j.1365-313X.2007.03192.x;
Nuehse T.S., Bottrill A.R., Jones A.M., Peck S.C.;
"Quantitative phosphoproteomic analysis of plasma membrane proteins
reveals regulatory mechanisms of plant innate immune responses.";
Plant J. 51:931-940(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND 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).
[15]
INTERACTION WITH BIK1 AND FLS2, IDENTIFICATION BY MASS SPECTROMETRY,
AND PHOSPHORYLATION AT SER-39; SER-343 AND SER-347.
PubMed=24629339; DOI=10.1016/j.chom.2014.02.009;
Li L., Li M., Yu L., Zhou Z., Liang X., Liu Z., Cai G., Gao L.,
Zhang X., Wang Y., Chen S., Zhou J.M.;
"The FLS2-associated kinase BIK1 directly phosphorylates the NADPH
oxidase RbohD to control plant immunity.";
Cell Host Microbe 15:329-338(2014).
[16]
INTERACTION WITH PBL13.
PubMed=26432875; DOI=10.1104/pp.15.01391;
Lin Z.J., Liebrand T.W., Yadeta K.A., Coaker G.;
"PBL13 is a serine/threonine protein kinase that negatively regulates
Arabidopsis immune responses.";
Plant Physiol. 169:2950-2962(2015).
-!- FUNCTION: Calcium-dependent NADPH oxidase that generates
superoxide. Involved in the generation of reactive oxygen species
(ROS) during incompatible interactions with pathogens and in UV-B
and abscisic acid ROS-dependent signaling. Might be required for
ROS signal amplification during light stress.
{ECO:0000269|PubMed:11756663, ECO:0000269|PubMed:12773379,
ECO:0000269|PubMed:15608336, ECO:0000269|PubMed:16428598,
ECO:0000269|PubMed:16913867, ECO:0000269|PubMed:17601167}.
-!- ENZYME REGULATION: Inhibited by diphenylene iodinium (DPI).
{ECO:0000269|PubMed:17601167}.
-!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with
BIK1 and FLS2 (PubMed:24629339). Interacts with PBL13
(PubMed:26432875). {ECO:0000250, ECO:0000269|PubMed:24629339,
ECO:0000269|PubMed:26432875}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: More abundant in roots than in leaves, stems
or inflorescences. Expressed in mesophyll and guard cells.
{ECO:0000269|PubMed:12773379, ECO:0000269|PubMed:9628030}.
-!- INDUCTION: Up-regulated by pathogen infection and by abscisic
acid. {ECO:0000269|PubMed:12773379, ECO:0000269|PubMed:17601167}.
-!- PTM: Phosphorylated at Ser-39, Ser-343 and Ser-347 by BIK1 upon
flagellin (flg22) treatment. {ECO:0000269|PubMed:24629339}.
-!- DISRUPTION PHENOTYPE: Plants do not accumulate reactive oxygen
species during disease-resistance reactions, do not up-regulate
UV-B-dependent gene expression and are impaired in abscisic acid-
induced stomatal closing and in root growth and seed germination
inhibitions. {ECO:0000269|PubMed:15608336}.
-!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF055357; AAC39479.1; -; mRNA.
EMBL; AB016886; BAB11338.1; -; Genomic_DNA.
EMBL; CP002688; AED95593.1; -; Genomic_DNA.
EMBL; AF424625; AAL11618.1; -; mRNA.
EMBL; BT002651; AAO11567.1; -; mRNA.
PIR; T51804; T51804.
RefSeq; NP_199602.1; NM_124165.3.
UniGene; At.23270; -.
ProteinModelPortal; Q9FIJ0; -.
SMR; Q9FIJ0; -.
BioGrid; 20090; 38.
STRING; 3702.AT5G47910.1; -.
PeroxiBase; 3286; AtRboh04.
iPTMnet; Q9FIJ0; -.
PaxDb; Q9FIJ0; -.
PRIDE; Q9FIJ0; -.
EnsemblPlants; AT5G47910.1; AT5G47910.1; AT5G47910.
GeneID; 834842; -.
Gramene; AT5G47910.1; AT5G47910.1; AT5G47910.
KEGG; ath:AT5G47910; -.
Araport; AT5G47910; -.
TAIR; locus:2160917; AT5G47910.
eggNOG; KOG0039; Eukaryota.
eggNOG; ENOG410XNZY; LUCA.
HOGENOM; HOG000216670; -.
InParanoid; Q9FIJ0; -.
KO; K13447; -.
OMA; GINGPFG; -.
OrthoDB; EOG093601IF; -.
PhylomeDB; Q9FIJ0; -.
BioCyc; ARA:AT5G47910-MONOMER; -.
BRENDA; 1.6.3.1; 399.
Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q9FIJ0; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q9FIJ0; AT.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0016174; F:NAD(P)H oxidase activity; IMP:TAIR.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0033500; P:carbohydrate homeostasis; IMP:TAIR.
GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
GO; GO:0043069; P:negative regulation of programmed cell death; IGI:TAIR.
GO; GO:0007231; P:osmosensory signaling pathway; IMP:TAIR.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
GO; GO:0009408; P:response to heat; IMP:TAIR.
GO; GO:0009611; P:response to wounding; IEP:TAIR.
CDD; cd00051; EFh; 1.
InterPro; IPR000778; Cyt_b245_heavy_chain.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR013623; NADPH_Ox.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
Pfam; PF08414; NADPH_Ox; 1.
PRINTS; PR00466; GP91PHOX.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 2.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
Calcium; Complete proteome; FAD; Flavoprotein; Membrane;
Metal-binding; NADP; Oxidoreductase; Peroxidase; Phosphoprotein;
Plant defense; Reference proteome; Repeat; Transmembrane;
Transmembrane helix.
CHAIN 1 921 Respiratory burst oxidase homolog protein
D.
/FTId=PRO_0000313756.
TOPO_DOM 1 376 Cytoplasmic. {ECO:0000255}.
TRANSMEM 377 397 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 398 461 Extracellular. {ECO:0000255}.
TRANSMEM 462 482 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 483 516 Cytoplasmic. {ECO:0000255}.
TRANSMEM 517 537 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 538 559 Extracellular. {ECO:0000255}.
TRANSMEM 560 580 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 581 588 Cytoplasmic. {ECO:0000255}.
TRANSMEM 589 606 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 607 734 Extracellular. {ECO:0000255}.
TRANSMEM 735 755 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 756 921 Cytoplasmic. {ECO:0000255}.
DOMAIN 253 288 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 297 332 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 415 572 Ferric oxidoreductase.
DOMAIN 611 732 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
CA_BIND 266 277 {ECO:0000255|PROSITE-ProRule:PRU00448}.
REGION 193 203 EF-hand-like 1. {ECO:0000250}.
REGION 230 241 EF-hand-like 2. {ECO:0000250}.
COMPBIAS 98 101 Poly-Gly.
METAL 266 266 Calcium. {ECO:0000250}.
METAL 268 268 Calcium. {ECO:0000250}.
METAL 270 270 Calcium. {ECO:0000250}.
METAL 272 272 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 277 277 Calcium. {ECO:0000250}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:17651370}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:19245862,
ECO:0000244|PubMed:19376835,
ECO:0000269|PubMed:24629339}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000244|PubMed:17651370,
ECO:0000269|PubMed:24629339}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000244|PubMed:17651370,
ECO:0000269|PubMed:24629339}.
SEQUENCE 921 AA; 103909 MW; 1A822569A7AB1817 CRC64;
MKMRRGNSSN DHELGILRGA NSDTNSDTES IASDRGAFSG PLGRPKRASK KNARFADDLP
KRSNSVAGGR GDDDEYVEIT LDIRDDSVAV HSVQQAAGGG GHLEDPELAL LTKKTLESSL
NNTTSLSFFR STSSRIKNAS RELRRVFSRR PSPAVRRFDR TSSAAIHALK GLKFIATKTA
AWPAVDQRFD KLSADSNGLL LSAKFWECLG MNKESKDFAD QLFRALARRN NVSGDAITKE
QLRIFWEQIS DESFDAKLQV FFDMVDKDED GRVTEEEVAE IISLSASANK LSNIQKQAKE
YAALIMEELD PDNAGFIMIE NLEMLLLQAP NQSVRMGDSR ILSQMLSQKL RPAKESNPLV
RWSEKIKYFI LDNWQRLWIM MLWLGICGGL FTYKFIQYKN KAAYGVMGYC VCVAKGGAET
LKFNMALILL PVCRNTITWL RNKTKLGTVV PFDDSLNFHK VIASGIVVGV LLHAGAHLTC
DFPRLIAADE DTYEPMEKYF GDQPTSYWWF VKGVEGWTGI VMVVLMAIAF TLATPWFRRN
KLNLPNFLKK LTGFNAFWYT HHLFIIVYAL LIVHGIKLYL TKIWYQKTTW MYLAVPILLY
ASERLLRAFR SSIKPVKMIK VAVYPGNVLS LHMTKPQGFK YKSGQFMLVN CRAVSPFEWH
PFSITSAPGD DYLSVHIRTL GDWTRKLRTV FSEVCKPPTA GKSGLLRADG GDGNLPFPKV
LIDGPYGAPA QDYKKYDVVL LVGLGIGATP MISILKDIIN NMKGPDRDSD IENNNSNNNS
KGFKTRKAYF YWVTREQGSF EWFKGIMDEI SELDEEGIIE LHNYCTSVYE EGDARVALIA
MLQSLQHAKN GVDVVSGTRV KSHFAKPNWR QVYKKIAVQH PGKRIGVFYC GMPGMIKELK
NLALDFSRKT TTKFDFHKEN F


Related products :

Catalog number Product name Quantity
EIAAB27575 Kidney oxidase-1,Kidney superoxide-producing NADPH oxidase,KOX-1,Mouse,Mus musculus,NADPH oxidase 4,Nox4,Renal NAD(P)H-oxidase,Renox,Superoxide-generating NADPH oxidase 4
EIAAB27574 Homo sapiens,Human,Kidney oxidase-1,Kidney superoxide-producing NADPH oxidase,KOX-1,NADPH oxidase 4,NOX4,Renal NAD(P)H-oxidase,RENOX
EIAAB27573 Kidney oxidase-1,Kidney superoxide-producing NADPH oxidase,Kox,KOX-1,NADPH oxidase 4,Nox4,Rat,Rattus norvegicus
EIAAB12031 Dual oxidase 2,DUOX2,Homo sapiens,Human,Large NOX 2,LNOX2,Long NOX 2,NADH_NADPH thyroid oxidase p138-tox,NADPH oxidase_peroxidase DUOX2,NADPH thyroid oxidase 2,p138 thyroid oxidase,THOX2,Thyroid oxida
EIAAB27571 GP91-3,gp91phox homolog 3,Homo sapiens,Human,Mitogenic oxidase 2,MOX2,MOX-2,NADPH oxidase 3,NOX3
EIAAB27582 Homo sapiens,Human,NADPH oxidase organizer 1,NADPH oxidase regulatory protein,Nox organizer 1,NOXO1,Nox-organizing protein 1,P41NOX,SH3 and PX domain-containing protein 5,SH3PXD5
EIAAB26522 67 kDa neutrophil oxidase factor,Homo sapiens,Human,NADPH oxidase activator 2,NCF2,NCF-2,Neutrophil cytosol factor 2,Neutrophil NADPH oxidase factor 2,NOXA2,P67PHOX,p67-phox
EIAAB26524 67 kDa neutrophil oxidase factor,Mouse,Mus musculus,NADPH oxidase activator 2,Ncf2,NCF-2,Neutrophil cytosol factor 2,Neutrophil NADPH oxidase factor 2,Noxa2,P67phox,p67-phox
EIAAB27568 Homo sapiens,Human,Mitogenic oxidase 1,MOX1,MOX-1,NADH_NADPH mitogenic oxidase subunit P65-MOX,NADPH oxidase 1,NOH1,NOH-1,NOX1,NOX-1
EIAAB12028 Dual oxidase 1,DUOX,DUOX1,Homo sapiens,Human,Large NOX 1,LNOX1,Long NOX 1,NADPH thyroid oxidase 1,THOX1,Thyroid oxidase 1
EIAAB27569 Mitogenic oxidase 1,Mox1,MOX-1,NADH_NADPH mitogenic oxidase subunit P65-MOX,NADPH oxidase 1,Noh1,NOH-1,Nox1,NOX-1,Rat,Rattus norvegicus
EIAAB12030 Canis familiaris,Canis lupus familiaris,Dog,Dual oxidase 1,DUOX1,NADPH thyroid oxidase 1,THOX1,Thyroid oxidase 1
LF-PA40830 anti-NADPH Oxidase Organizer 1 (NOXO1) , Goat polyclonal to NADPH Oxidase Organizer 1 (NOXO1) , Isotype IgG, Host Goat 100
LF-PA40831 anti-NADPH Oxidase Organizer 1 (NOXO1) , Rabbit polyclonal to NADPH Oxidase Organizer 1 (NOXO1) , Isotype IgG, Host Rabbit 50 ug
EIAAB26517 47 kDa autosomal chronic granulomatous disease protein,47 kDa neutrophil oxidase factor,Homo sapiens,Human,NCF1,NCF-1,NCF-47K,Neutrophil cytosol factor 1,Neutrophil NADPH oxidase factor 1,Nox organize
EIAAB32432 Kidney and liver proline oxidase 1,MmPOX1,Mouse,Mus musculus,PO,Probable proline dehydrogenase 2,Probable proline oxidase 2,Prodh2,Proline oxidase,Proline oxidase-like protein
EIAAB39256 Bos taurus,Bovine,L-pipecolate oxidase,L-pipecolic acid oxidase,Peroxisomal sarcosine oxidase,PIPOX,PSO
EIAAB39255 L-pipecolate oxidase,L-pipecolic acid oxidase,Mouse,Mus musculus,Peroxisomal sarcosine oxidase,Pipox,PSO,Pso
EIAAB39254 L-pipecolate oxidase,L-pipecolic acid oxidase,Oryctolagus cuniculus,Peroxisomal sarcosine oxidase,PIPOX,PSO,PSO,Rabbit,SOX
EIAAB39257 Homo sapiens,Human,L-pipecolate oxidase,L-pipecolic acid oxidase,LPIPOX,Peroxisomal sarcosine oxidase,PIPOX,PSO,PSO
E0656h ELISA ABP,ABP1,Amiloride-binding protein,Amiloride-sensitive amine oxidase [copper-containing],AOC1,DAO,DAO1,Diamine oxidase,Histaminase,Homo sapiens,Human,KAO,Kidney amine oxidase 96T
E0656h ELISA kit ABP,ABP1,Amiloride-binding protein,Amiloride-sensitive amine oxidase [copper-containing],AOC1,DAO,DAO1,Diamine oxidase,Histaminase,Homo sapiens,Human,KAO,Kidney amine oxidase 96T
U0656h CLIA ABP,ABP1,Amiloride-binding protein,Amiloride-sensitive amine oxidase [copper-containing],AOC1,DAO,DAO1,Diamine oxidase,Histaminase,Homo sapiens,Human,KAO,Kidney amine oxidase 96T
EIAAB26518 47 kDa neutrophil oxidase factor,Mouse,Mus musculus,Ncf1,NCF-1,NCF-47K,Neutrophil cytosol factor 1,Neutrophil NADPH oxidase factor 1,p47-phox
EIAAB26516 47 kDa neutrophil oxidase factor,Bos taurus,Bovine,NCF1,NCF-1,NCF-47K,Neutrophil cytosol factor 1,Neutrophil NADPH oxidase factor 1,p47-phox


 

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