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 F (EC 1.11.1.-) (EC 1.6.3.-) (Cytochrome b245 beta chain homolog RbohAp108) (NADPH oxidase RBOHF) (AtRBOHF)

 RBOHF_ARATH             Reviewed;         944 AA.
O48538; O80342; Q0WR97; Q9SH56;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 125.
RecName: Full=Respiratory burst oxidase homolog protein F;
EC=1.11.1.-;
EC=1.6.3.-;
AltName: Full=Cytochrome b245 beta chain homolog RbohAp108;
AltName: Full=NADPH oxidase RBOHF;
Short=AtRBOHF;
Name=RBOHF; Synonyms=RBOHAP108; OrderedLocusNames=At1g64060;
ORFNames=F22C12.18;
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 [MRNA], PROTEIN SEQUENCE OF 2-3, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, CALCIUM-BINDING DATA, AND LACK OF
GLYCOSYLATION.
STRAIN=cv. Columbia;
PubMed=9490748; DOI=10.1105/tpc.10.2.255;
Keller T., Damude H.G., Werner D., Doerner P., Dixon R.A., Lamb C.;
"A plant homolog of the neutrophil NADPH oxidase gp91phox subunit gene
encodes a plasma membrane protein with Ca2+ binding motifs.";
Plant Cell 10:255-266(1998).
[3]
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).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
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).
[7]
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).
[8]
FUNCTION, AND ENZYME REGULATION.
PubMed=16961732; DOI=10.1111/j.1365-313X.2006.02842.x;
Desikan R., Last K., Harrett-Williams R., Tagliavia C., Harter K.,
Hooley R., Hancock J.T., Neill S.J.;
"Ethylene-induced stomatal closure in Arabidopsis occurs via AtrbohF-
mediated hydrogen peroxide synthesis.";
Plant J. 47:907-916(2006).
[9]
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).
[10]
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).
[11]
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).
[12]
INTERACTION WITH SRC2.
PubMed=23872431; DOI=10.1016/j.bbamcr.2013.06.024;
Kawarazaki T., Kimura S., Iizuka A., Hanamata S., Nibori H.,
Michikawa M., Imai A., Abe M., Kaya H., Kuchitsu K.;
"A low temperature-inducible protein AtSRC2 enhances the ROS-producing
activity of NADPH oxidase AtRbohF.";
Biochim. Biophys. Acta 1833:2775-2780(2013).
[13]
INTERACTION WITH CIPK26, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=23335733; DOI=10.1093/mp/sst009;
Drerup M.M., Schluecking K., Hashimoto K., Manishankar P.,
Steinhorst L., Kuchitsu K., Kudla J.;
"The Calcineurin B-like calcium sensors CBL1 and CBL9 together with
their interacting protein kinase CIPK26 regulate the Arabidopsis NADPH
oxidase RBOHF.";
Mol. Plant 6:559-569(2013).
-!- FUNCTION: Calcium-dependent NADPH oxidase that generates
superoxide. Generates reactive oxygen species (ROS) during
incompatible interactions with pathogens and is important in the
regulation of the hypersensitive response (HR). Involved in
abscisic acid-induced stomatal closing and in UV-B and abscisic
acid ROS-dependent signaling. {ECO:0000269|PubMed:11756663,
ECO:0000269|PubMed:12773379, ECO:0000269|PubMed:16428598,
ECO:0000269|PubMed:16913867, ECO:0000269|PubMed:16961732}.
-!- ENZYME REGULATION: Inhibited by diphenylene iodonium (DPI).
{ECO:0000269|PubMed:16961732}.
-!- SUBUNIT: Monomer and homodimer (By similarity). Interacts (via N-
terminus) with CIPK26 (PubMed:23335733). Interacts (via N-
terminus) with SRC2 (PubMed:23872431). {ECO:0000250,
ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:23872431}.
-!- INTERACTION:
Q940H6:SRK2E; NbExp=4; IntAct=EBI-7197253, EBI-782514;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23335733,
ECO:0000269|PubMed:9490748}; Multi-pass membrane protein
{ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:9490748}.
-!- TISSUE SPECIFICITY: Expressed in roots, stems, seedlings,
inflorescences, leaves and guard cells.
{ECO:0000269|PubMed:12773379, ECO:0000269|PubMed:9490748,
ECO:0000269|PubMed:9628030}.
-!- INDUCTION: Up-regulated by abscisic acid.
{ECO:0000269|PubMed:12773379}.
-!- PTM: Not glycosylated. Phosphorylated by CIPK26.
{ECO:0000269|PubMed:23335733}.
-!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.
{ECO:0000305}.
-!- CAUTION: Was originally called RBOHA.
{ECO:0000305|PubMed:9490748}.
-!- SEQUENCE CAUTION:
Sequence=AAF24574.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAF00352.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB008111; BAA28953.1; -; mRNA.
EMBL; AF015301; AAB87789.1; -; mRNA.
EMBL; AC007764; AAF24574.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE34186.1; -; Genomic_DNA.
EMBL; AK228418; BAF00352.1; ALT_SEQ; mRNA.
PIR; T03826; T03826.
RefSeq; NP_564821.1; NM_105079.3.
UniGene; At.235; -.
ProteinModelPortal; O48538; -.
BioGrid; 27931; 3.
IntAct; O48538; 1.
MINT; MINT-7260067; -.
STRING; 3702.AT1G64060.1; -.
TCDB; 5.B.1.1.9; the phagocyte (gp91(phox)) nadph oxidase family.
PaxDb; O48538; -.
PRIDE; O48538; -.
EnsemblPlants; AT1G64060.1; AT1G64060.1; AT1G64060.
GeneID; 842710; -.
Gramene; AT1G64060.1; AT1G64060.1; AT1G64060.
KEGG; ath:AT1G64060; -.
Araport; AT1G64060; -.
TAIR; locus:2024603; AT1G64060.
eggNOG; KOG0039; Eukaryota.
eggNOG; ENOG410XNZY; LUCA.
HOGENOM; HOG000216670; -.
InParanoid; O48538; -.
KO; K13447; -.
OMA; FDCSFIA; -.
OrthoDB; EOG093601IF; -.
PhylomeDB; O48538; -.
BioCyc; ARA:AT1G64060-MONOMER; -.
Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:O48538; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; O48538; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
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:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
GO; GO:0033500; P:carbohydrate homeostasis; IMP:TAIR.
GO; GO:0052542; P:defense response by callose deposition; IMP:TAIR.
GO; GO:0009873; P:ethylene-activated signaling pathway; TAS:TAIR.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:TAIR.
GO; GO:0043069; P:negative regulation of programmed cell death; IMP:TAIR.
GO; GO:0007231; P:osmosensory signaling pathway; IMP:TAIR.
GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
GO; GO:0002679; P:respiratory burst involved in defense response; IMP:TAIR.
GO; GO:0009723; P:response to ethylene; IMP:TAIR.
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; 1.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
Calcium; Cell membrane; Coiled coil; Complete proteome;
Direct protein sequencing; FAD; Flavoprotein; Membrane; Metal-binding;
NADP; Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome;
Repeat; Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9490748}.
CHAIN 2 944 Respiratory burst oxidase homolog protein
F.
/FTId=PRO_0000313758.
TOPO_DOM 2 387 Cytoplasmic. {ECO:0000255}.
TRANSMEM 388 408 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 409 475 Extracellular. {ECO:0000255}.
TRANSMEM 476 492 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 493 527 Cytoplasmic. {ECO:0000255}.
TRANSMEM 528 548 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 549 570 Extracellular. {ECO:0000255}.
TRANSMEM 571 591 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 592 599 Cytoplasmic. {ECO:0000255}.
TRANSMEM 600 617 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 618 744 Extracellular. {ECO:0000255}.
TRANSMEM 745 765 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 766 944 Cytoplasmic. {ECO:0000255}.
DOMAIN 264 299 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 308 343 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 426 583 Ferric oxidoreductase.
DOMAIN 622 742 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
CA_BIND 277 288 1. {ECO:0000269|PubMed:9490748}.
CA_BIND 321 332 2. {ECO:0000269|PubMed:9490748}.
REGION 207 215 EF-hand-like 1. {ECO:0000250}.
REGION 241 252 EF-hand-like 2. {ECO:0000250}.
COILED 102 126 {ECO:0000255}.
COILED 157 184 {ECO:0000255}.
COMPBIAS 239 242 Poly-Arg.
METAL 277 277 Calcium. {ECO:0000250}.
METAL 279 279 Calcium. {ECO:0000250}.
METAL 281 281 Calcium. {ECO:0000250}.
METAL 283 283 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 288 288 Calcium. {ECO:0000250}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000250|UniProtKB:Q9FIJ0}.
MOD_RES 358 358 Phosphoserine.
{ECO:0000250|UniProtKB:Q9FIJ0}.
CONFLICT 908 908 I -> T (in Ref. 1; BAA28953).
{ECO:0000305}.
SEQUENCE 944 AA; 108418 MW; 1ABAEC316AE80F9B CRC64;
MKPFSKNDRR RWSFDSVSAG KTAVGSASTS PGTEYSINGD QEFVEVTIDL QDDDTIVLRS
VEPATAINVI GDISDDNTGI MTPVSISRSP TMKRTSSNRF RQFSQELKAE AVAKAKQLSQ
ELKRFSWSRS FSGNLTTTST AANQSGGAGG GLVNSALEAR ALRKQRAQLD RTRSSAQRAL
RGLRFISNKQ KNVDGWNDVQ SNFEKFEKNG YIYRSDFAQC IGMKDSKEFA LELFDALSRR
RRLKVEKINH DELYEYWSQI NDESFDSRLQ IFFDIVDKNE DGRITEEEVK EIIMLSASAN
KLSRLKEQAE EYAALIMEEL DPERLGYIEL WQLETLLLQK DTYLNYSQAL SYTSQALSQN
LQGLRGKSRI HRMSSDFVYI MQENWKRIWV LSLWIMIMIG LFLWKFFQYK QKDAFHVMGY
CLLTAKGAAE TLKFNMALIL FPVCRNTITW LRSTRLSYFV PFDDNINFHK TIAGAIVVAV
ILHIGDHLAC DFPRIVRATE YDYNRYLFHY FQTKQPTYFD LVKGPEGITG ILMVILMIIS
FTLATRWFRR NLVKLPKPFD RLTGFNAFWY SHHLFVIVYI LLILHGIFLY FAKPWYVRTT
WMYLAVPVLL YGGERTLRYF RSGSYSVRLL KVAIYPGNVL TLQMSKPTQF RYKSGQYMFV
QCPAVSPFEW HPFSITSAPE DDYISIHIRQ LGDWTQELKR VFSEVCEPPV GGKSGLLRAD
ETTKKSLPKL LIDGPYGAPA QDYRKYDVLL LVGLGIGATP FISILKDLLN NIVKMEEHAD
SISDFSRSSE YSTGSNGDTP RRKRILKTTN AYFYWVTREQ GSFDWFKGVM NEVAELDQRG
VIEMHNYLTS VYEEGDARSA LITMVQALNH AKNGVDIVSG TRVRTHFARP NWKKVLTKLS
SKHCNARIGV FYCGVPVLGK ELSKLCNTFN QKGSTKFEFH KEHF


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
EIAAB27571 GP91-3,gp91phox homolog 3,Homo sapiens,Human,Mitogenic oxidase 2,MOX2,MOX-2,NADPH oxidase 3,NOX3
EIAAB27574 Homo sapiens,Human,Kidney oxidase-1,Kidney superoxide-producing NADPH oxidase,KOX-1,NADPH oxidase 4,NOX4,Renal NAD(P)H-oxidase,RENOX
EIAAB10225 CGD91-phox,CYBB,Cytochrome b(558) subunit beta,Cytochrome b-245 heavy chain,Cytochrome b558 subunit beta,gp91-1,gp91-phox,Heme-binding membrane glycoprotein gp91phox,Homo sapiens,Human,NADPH oxidase 2
EIAAB08789 COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-liver_heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Oryctolagus cuniculus,Rabb
EIAAB08785 Bos taurus,Bovine,COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,IX,VIIIb
EIAAB08787 Cox8b,Cox8h,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Mouse,Mus musculus
EIAAB08788 Cox8b,Cox8h,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Rat,Rattus norvegicus
EIAAB27573 Kidney oxidase-1,Kidney superoxide-producing NADPH oxidase,Kox,KOX-1,NADPH oxidase 4,Nox4,Rat,Rattus norvegicus
26-032 Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. COX10 is heme A farnesyltransferase, wh 0.05 mg
EIAAB10091 Bos taurus,Bovine,COX VIb-1,COX6B,COX6B1,Cytochrome c oxidase polypeptide VII,Cytochrome c oxidase subunit 6B1,Cytochrome c oxidase subunit AED,Cytochrome c oxidase subunit VIb isoform 1
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
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
EIAAB08786 Canis familiaris,Canis lupus familiaris,COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase sub
EIAAB10105 COX7A2,COX7AL,Cytochrome c oxidase subunit 7A2, mitochondrial,Cytochrome c oxidase subunit VIIaL,Cytochrome c oxidase subunit VIIa-L,Cytochrome c oxidase subunit VIIa-liver_heart,Homo sapiens,Human
EIAAB10086 COX VIa-M,COX6A,COX6A2,COX6AH,COXVIAH,Cytochrome c oxidase polypeptide VIa-heart,Cytochrome c oxidase subunit 6A2, mitochondrial,Cytochrome c oxidase subunit VIA-muscle,Homo sapiens,Human
EIAAB08781 COX8,COX8A,COX8L,Cytochrome c oxidase polypeptide VIII-liver_heart,Cytochrome c oxidase subunit 8-2,Cytochrome c oxidase subunit 8A, mitochondrial,Homo sapiens,Human
COX15_BOVIN Bovine ELISA Kit FOR Cytochrome c oxidase assembly protein COX15 homolog 96T
EIAAB08782 Bos taurus,Bovine,COX8,COX8A,COX8L,Cytochrome c oxidase polypeptide VIII-liver,Cytochrome c oxidase subunit 8-2,Cytochrome c oxidase subunit 8A, mitochondrial,IX
EIAAB08783 Cox8,Cox8a,Cox8l,Cytochrome c oxidase polypeptide VIII-liver,Cytochrome c oxidase subunit 8-2,Cytochrome c oxidase subunit 8A, mitochondrial,Rat,Rattus norvegicus
EIAAB08784 Cox8,Cox8a,Cox8l,Cytochrome c oxidase polypeptide VIII-liver,Cytochrome c oxidase subunit 8-2,Cytochrome c oxidase subunit 8A, mitochondrial,Mouse,Mus musculus
EIAAB10101 COX7A1,COX7AH,Cytochrome c oxidase subunit 7A1, mitochondrial,Cytochrome c oxidase subunit VIIa-H,Cytochrome c oxidase subunit VIIa-heart,Cytochrome c oxidase subunit VIIa-M,Cytochrome c oxidase subun
EIAAB10102 Cox7a,Cox7a1,Cox7ah,Cytochrome c oxidase subunit 7A1, mitochondrial,Cytochrome c oxidase subunit VIIa-H,Cytochrome c oxidase subunit VIIa-heart,Cytochrome c oxidase subunit VIIa-M,Cytochrome c oxidase
EIAAB10087 Bos taurus,Bovine,COX6A,COX6A2,COXVIAH,Cytochrome c oxidase polypeptide VIa-heart,Cytochrome c oxidase polypeptide VIb,Cytochrome c oxidase subunit 6A2, mitochondrial
EIAAB08773 Cox7c,Cox7c1,Cytochrome c oxidase polypeptide VIIc,Cytochrome c oxidase polypeptide VIIIA,Cytochrome c oxidase subunit 7C, mitochondrial,Rat,Rattus norvegicus


 

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