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NADPH oxidase activator 1 (NOX activator 1) (Antigen NY-CO-31) (NCF2-like protein) (P67phox-like factor) (p51-nox)

 NOXA1_HUMAN             Reviewed;         476 AA.
Q86UR1; O60533; Q29VU9; Q29VV0; Q2TAM1; Q8IUS3;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
31-JAN-2018, entry version 133.
RecName: Full=NADPH oxidase activator 1;
Short=NOX activator 1;
AltName: Full=Antigen NY-CO-31;
AltName: Full=NCF2-like protein;
AltName: Full=P67phox-like factor;
AltName: Full=p51-nox;
Name=NOXA1; Synonyms=P51NOX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS NOX1
ACTIVATOR.
TISSUE=Kidney;
PubMed=12657628; DOI=10.1074/jbc.M301289200;
Geiszt M., Lekstrom K., Witta J., Leto T.L.;
"Proteins homologous to p47phox and p67phox support superoxide
production by NAD(P)H oxidase 1 in colon epithelial cells.";
J. Biol. Chem. 278:20006-20012(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS NOX1 ACTIVATOR,
INTERACTION WITH NCF1; NOXO1 AND RAC1, MUTAGENESIS OF ARG-103 AND
TRP-436, AND TISSUE SPECIFICITY.
PubMed=12716910; DOI=10.1074/jbc.M212856200;
Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H.,
Sumimoto H.;
"Novel human homologues of p47phox and p67phox participate in
activation of superoxide-producing NADPH oxidases.";
J. Biol. Chem. 278:25234-25246(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION AS NOX1 ACTIVATOR,
MUTAGENESIS OF PRO-34; PRO-37 AND TRP-436, AND VARIANTS LEU-286 AND
NOXA1TRUNCATED.
TISSUE=Colon adenocarcinoma;
PubMed=17602954; DOI=10.1016/j.freeradbiomed.2007.04.022;
Valente A.J., Jamali A.E., Epperson T.K., Gamez M.J., Pearson D.W.,
Clark R.A.;
"NOX1 NADPH oxidase regulation by the NOXA1 SH3 domain.";
Free Radic. Biol. Med. 43:384-396(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 245-476 (ISOFORM 1).
TISSUE=Colon cancer;
PubMed=9610721;
DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P;
Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
"Characterization of human colon cancer antigens recognized by
autologous antibodies.";
Int. J. Cancer 76:652-658(1998).
[7]
FUNCTION AS NOX1 ACTIVATOR.
PubMed=14617635; DOI=10.1074/jbc.M305968200;
Cheng G., Lambeth J.D.;
"NOXO1, regulation of lipid binding, localization, and activation of
Nox1 by the Phox homology (PX) domain.";
J. Biol. Chem. 279:4737-4742(2004).
[8]
FUNCTION AS CYBB AND NOX3 ACTIVATOR, AND MUTAGENESIS OF VAL-205.
PubMed=15181005; DOI=10.1074/jbc.M400660200;
Cheng G., Ritsick D., Lambeth J.D.;
"Nox3 regulation by NOXO1, p47phox, and p67phox.";
J. Biol. Chem. 279:34250-34255(2004).
[9]
FUNCTION.
PubMed=14978110; DOI=10.4049/jimmunol.172.5.3051;
Kawahara T., Kuwano Y., Teshima-Kondo S., Takeya R., Sumimoto H.,
Kishi K., Tsunawaki S., Hirayama T., Rokutan K.;
"Role of nicotinamide adenine dinucleotide phosphate oxidase 1 in
oxidative burst response to Toll-like receptor 5 signaling in large
intestinal epithelial cells.";
J. Immunol. 172:3051-3058(2004).
[10]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=15824103; DOI=10.1074/jbc.M414548200;
Ueno N., Takeya R., Miyano K., Kikuchi H., Sumimoto H.;
"The NADPH oxidase Nox3 constitutively produces superoxide in a
p22phox-dependent manner: its regulation by oxidase organizers and
activators.";
J. Biol. Chem. 280:23328-23339(2005).
[11]
IDENTIFICATION IN A COMPLEX CONTAINING NOX1; NOXO1; NOXA1 AND RAC1,
AND MUTAGENESIS OF ASP-68 AND ARG-103.
PubMed=16636067; DOI=10.1074/jbc.M512751200;
Cheng G., Diebold B.A., Hughes Y., Lambeth J.D.;
"Nox1-dependent reactive oxygen generation is regulated by Rac1.";
J. Biol. Chem. 281:17718-17726(2006).
[12]
SUBCELLULAR LOCATION, INTERACTION WITH RAC1, AND MUTAGENESIS OF
ARG-103 AND TRP-436.
PubMed=16762923; DOI=10.1074/jbc.M513665200;
Miyano K., Ueno N., Takeya R., Sumimoto H.;
"Direct involvement of the small GTPase Rac in activation of the
superoxide-producing NADPH oxidase Nox1.";
J. Biol. Chem. 281:21857-21868(2006).
[13]
CHARACTERIZATION OF THE FUNCTIONAL NOX1 OXIDASE COMPLEX, AND
SUBCELLULAR LOCATION.
PubMed=16507994; DOI=10.1128/MCB.26.6.2160-2174.2006;
Ueyama T., Geiszt M., Leto T.L.;
"Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-
based NADPH oxidases.";
Mol. Cell. Biol. 26:2160-2174(2006).
[14]
INTERACTION WITH NOXO1.
PubMed=17126813; DOI=10.1016/j.bbrc.2006.11.060;
Yamamoto A., Kami K., Takeya R., Sumimoto H.;
"Interaction between the SH3 domains and C-terminal proline-rich
region in NADPH oxidase organizer 1 (Noxo1).";
Biochem. Biophys. Res. Commun. 352:560-565(2007).
[15]
INTERACTION WITH YWHAZ, MUTAGENESIS OF SER-172 AND SER-461, AND
PHOSPHORYLATION AT SER-172 AND SER-461.
PubMed=17913709; DOI=10.1074/jbc.M704754200;
Kim J.-S., Diebold B.A., Babior B.M., Knaus U.G., Bokoch G.M.;
"Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1
and 14-3-3 binding.";
J. Biol. Chem. 282:34787-34800(2007).
[16]
FUNCTION, AND INTERACTION WITH SH3PXD2A AND SH3PXD2B.
PubMed=19755710; DOI=10.1126/scisignal.2000370;
Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A.,
Bokoch G.M.;
"Novel p47(phox)-related organizers regulate localized NADPH oxidase 1
(Nox1) activity.";
Sci. Signal. 2:RA54-RA54(2009).
[17]
INTERACTION WITH SH3PXD2A AND SH3PXD2B.
PubMed=20609497; DOI=10.1016/j.ejcb.2010.05.007;
Gianni D., Dermardirossian C., Bokoch G.M.;
"Direct interaction between Tks proteins and the N-terminal proline-
rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation.";
Eur. J. Cell Biol. 90:164-171(2011).
-!- FUNCTION: Functions as an activator of NOX1, a superoxide-
producing NADPH oxidase. Functions in the production of reactive
oxygen species (ROS) which participate in a variety of biological
processes including host defense, hormone biosynthesis, oxygen
sensing and signal transduction. May also activate CYBB/gp91phox
and NOX3. {ECO:0000269|PubMed:12657628,
ECO:0000269|PubMed:12716910, ECO:0000269|PubMed:14617635,
ECO:0000269|PubMed:14978110, ECO:0000269|PubMed:15181005,
ECO:0000269|PubMed:15824103, ECO:0000269|PubMed:17602954,
ECO:0000269|PubMed:19755710}.
-!- SUBUNIT: NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional
multimeric complex supporting ROS production. Interaction with
YWHAZ prevents the interaction of NOXA1 with NOXO1 and RAC1 and
its targeting to membranes, hence reducing its ability to activate
NOX1. Interacts (via N-terminus) with SH3PXD2A and SH3PXD2B; the
interaction is direct. {ECO:0000269|PubMed:12716910,
ECO:0000269|PubMed:16636067, ECO:0000269|PubMed:16762923,
ECO:0000269|PubMed:17126813, ECO:0000269|PubMed:17913709,
ECO:0000269|PubMed:19755710, ECO:0000269|PubMed:20609497}.
-!- INTERACTION:
Q8NFA2:NOXO1; NbExp=6; IntAct=EBI-949814, EBI-7130806;
Q9UFD9:RIMBP3; NbExp=3; IntAct=EBI-949814, EBI-10182375;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocation
to membranes depends on NOXO1 or NCF1 and maybe RAC1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q86UR1-1; Sequence=Displayed;
Name=2;
IsoId=Q86UR1-2; Sequence=VSP_030336;
Note=Mostly inactive for NOX1 activation. Does not interact with
NOXO1.;
Name=3; Synonyms=NOXA1inhib;
IsoId=Q86UR1-3; Sequence=VSP_030335, VSP_030336;
Note=Inactive for NOX1 activation. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Widely expressed. Detected in pancreas, liver,
kidney, spleen, prostate, small intestine and colon.
{ECO:0000269|PubMed:12716910}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal kidney.
{ECO:0000269|PubMed:15824103}.
-!- DOMAIN: The SH3 domain mediates interaction with NOXO1 and NCF1
and has autoregulatory function.
-!- DOMAIN: The TPR repeats mediate interaction with RAC1.
-!- PTM: Interaction with YWHAZ depends on phosphorylation by PKA.
{ECO:0000269|PubMed:17913709}.
-!- SIMILARITY: Belongs to the NCF2/NOXA1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAY16126.1; Type=Frameshift; Positions=305; Evidence={ECO:0000305};
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EMBL; AY255769; AAP13480.1; -; mRNA.
EMBL; AB095031; BAC76710.1; -; mRNA.
EMBL; AY927790; AAY16126.1; ALT_FRAME; mRNA.
EMBL; AY927791; AAY16127.1; -; mRNA.
EMBL; BX322799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC041594; AAH41594.1; -; mRNA.
EMBL; BC110840; AAI10841.1; -; mRNA.
EMBL; AF039697; AAC18046.1; -; mRNA.
CCDS; CCDS59157.1; -. [Q86UR1-3]
CCDS; CCDS7042.1; -. [Q86UR1-2]
RefSeq; NP_001242996.1; NM_001256067.1. [Q86UR1-1]
RefSeq; NP_001242997.1; NM_001256068.1. [Q86UR1-3]
RefSeq; NP_006638.1; NM_006647.1. [Q86UR1-2]
UniGene; Hs.495554; -.
ProteinModelPortal; Q86UR1; -.
SMR; Q86UR1; -.
BioGrid; 116025; 13.
ELM; Q86UR1; -.
IntAct; Q86UR1; 43.
MINT; MINT-1211202; -.
STRING; 9606.ENSP00000342848; -.
iPTMnet; Q86UR1; -.
PhosphoSitePlus; Q86UR1; -.
BioMuta; NOXA1; -.
DMDM; 74759404; -.
PaxDb; Q86UR1; -.
PeptideAtlas; Q86UR1; -.
PRIDE; Q86UR1; -.
Ensembl; ENST00000341349; ENSP00000342848; ENSG00000188747. [Q86UR1-2]
Ensembl; ENST00000392815; ENSP00000376562; ENSG00000188747. [Q86UR1-3]
GeneID; 10811; -.
KEGG; hsa:10811; -.
UCSC; uc004cmu.4; human. [Q86UR1-1]
CTD; 10811; -.
DisGeNET; 10811; -.
EuPathDB; HostDB:ENSG00000188747.8; -.
GeneCards; NOXA1; -.
H-InvDB; HIX0018704; -.
HGNC; HGNC:10668; NOXA1.
HPA; HPA044781; -.
MIM; 611255; gene.
neXtProt; NX_Q86UR1; -.
OpenTargets; ENSG00000188747; -.
PharmGKB; PA35598; -.
eggNOG; KOG4225; Eukaryota.
eggNOG; ENOG41110AD; LUCA.
GeneTree; ENSGT00530000063843; -.
HOGENOM; HOG000237312; -.
HOVERGEN; HBG098043; -.
InParanoid; Q86UR1; -.
KO; K21432; -.
OMA; FQLERFQ; -.
OrthoDB; EOG091G04T7; -.
PhylomeDB; Q86UR1; -.
TreeFam; TF329087; -.
Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
SIGNOR; Q86UR1; -.
GeneWiki; NOXA1; -.
GenomeRNAi; 10811; -.
PRO; PR:Q86UR1; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000188747; -.
CleanEx; HS_NOXA1; -.
Genevisible; Q86UR1; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043020; C:NADPH oxidase complex; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0048365; F:Rac GTPase binding; IPI:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IDA:UniProtKB.
GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:BHF-UCL.
GO; GO:0060263; P:regulation of respiratory burst; IMP:BHF-UCL.
GO; GO:0006801; P:superoxide metabolic process; IMP:UniProtKB.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR034899; NOXA1.
InterPro; IPR000270; PB1_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR15175:SF4; PTHR15175:SF4; 1.
Pfam; PF00564; PB1; 1.
Pfam; PF00018; SH3_1; 1.
SMART; SM00666; PB1; 1.
SMART; SM00326; SH3; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51745; PB1; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
SH3 domain; TPR repeat.
CHAIN 1 476 NADPH oxidase activator 1.
/FTId=PRO_0000314609.
REPEAT 7 38 TPR 1.
REPEAT 39 71 TPR 2.
REPEAT 73 105 TPR 3.
REPEAT 122 155 TPR 4.
DOMAIN 315 395 PB1. {ECO:0000255|PROSITE-
ProRule:PRU01081}.
DOMAIN 399 458 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 1 224 Mediates interaction with RAC1.
MOD_RES 172 172 Phosphoserine; by PKA.
{ECO:0000269|PubMed:17913709}.
MOD_RES 461 461 Phosphoserine; by PKA.
{ECO:0000269|PubMed:17913709}.
VAR_SEQ 168 223 Missing (in isoform 3).
{ECO:0000303|PubMed:17602954}.
/FTId=VSP_030335.
VAR_SEQ 431 431 E -> EEPDVPLA (in isoform 2 and isoform
3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17602954}.
/FTId=VSP_030336.
VARIANT 274 476 Missing (found in a truncated form
isolated from Caco-2 cells treated with
butyrate).
/FTId=VAR_037985.
VARIANT 286 286 P -> L (in dbSNP:rs34155071).
{ECO:0000269|PubMed:17602954}.
/FTId=VAR_037986.
MUTAGEN 34 34 P->A: Partial loss of function.
{ECO:0000269|PubMed:17602954}.
MUTAGEN 37 37 P->A: Partial loss of function.
{ECO:0000269|PubMed:17602954}.
MUTAGEN 68 68 D->A: Loss of function and loss of
interaction with RAC1.
{ECO:0000269|PubMed:16636067}.
MUTAGEN 103 103 R->E: Loss of function and loss of
interaction with RAC1. Loss of
localization to membranes.
{ECO:0000269|PubMed:12716910,
ECO:0000269|PubMed:16636067,
ECO:0000269|PubMed:16762923}.
MUTAGEN 172 172 S->A: Loss of phosphorylation. Loss of
interaction with YHAWZ; when associated
with A-461.
{ECO:0000269|PubMed:17913709}.
MUTAGEN 172 172 S->E: Constitutively interacts with
YWHAZ; when associated with E-461.
{ECO:0000269|PubMed:17913709}.
MUTAGEN 205 205 V->A: Unable to activate NOX2.
{ECO:0000269|PubMed:15181005}.
MUTAGEN 436 436 W->R: Loss of interaction with NOXO1 and
NCF1. Loss of localization to membranes.
Partial loss of function.
{ECO:0000269|PubMed:12716910,
ECO:0000269|PubMed:16762923,
ECO:0000269|PubMed:17602954}.
MUTAGEN 461 461 S->A: Loss of phosphorylation. Loss of
interaction with YHAWZ; when associated
with A-172.
{ECO:0000269|PubMed:17913709}.
MUTAGEN 461 461 S->E: Constitutively interacts with
YWHAZ; when associated with E-172.
{ECO:0000269|PubMed:17913709}.
CONFLICT 51 51 A -> T (in Ref. 3; AAY16126).
{ECO:0000305}.
CONFLICT 56 56 A -> T (in Ref. 3; AAY16127).
{ECO:0000305}.
CONFLICT 73 73 V -> L (in Ref. 3; AAY16127).
{ECO:0000305}.
CONFLICT 142 142 A -> T (in Ref. 3; AAY16127).
{ECO:0000305}.
CONFLICT 261 261 T -> A (in Ref. 3; AAY16126).
{ECO:0000305}.
CONFLICT 277 277 K -> E (in Ref. 3; AAY16126).
{ECO:0000305}.
CONFLICT 278 278 Q -> V (in Ref. 6; AAC18046).
{ECO:0000305}.
CONFLICT 320 320 C -> R (in Ref. 3; AAY16127).
{ECO:0000305}.
CONFLICT 329 329 R -> G (in Ref. 6; AAC18046).
{ECO:0000305}.
CONFLICT 345 346 LP -> FL (in Ref. 6; AAC18046).
{ECO:0000305}.
CONFLICT 354 354 L -> F (in Ref. 6; AAC18046).
{ECO:0000305}.
CONFLICT 409 409 S -> R (in Ref. 6; AAC18046).
{ECO:0000305}.
CONFLICT 441 441 C -> R (in Ref. 5; AAI10841).
{ECO:0000305}.
SEQUENCE 476 AA; 50933 MW; 64DFBF64C59722AD CRC64;
MASLGDLVRA WHLGAQAVDR GDWARALHLF SGVPAPPARL CFNAGCVHLL AGDPEAALRA
FDQAVTKDTC MAVGFFQRGV ANFQLARFQE ALSDFWLALE QLRGHAAIDY TQLGLRFKLQ
AWEVLHNVAS AQCQLGLWTE AASSLREAMS KWPEGSLNGL DSALDQVQRR GSLPPRQVPR
GEVFRPHRWH LKHLEPVDFL GKAKVVASAI PDDQGWGVRP QQPQGPGANH DARSLIMDSP
RAGTHQGPLD AETEVGADRC TSTAYQEQRP QVEQVGKQAP LSPGLPAMGG PGPGPCEDPA
GAGGAGAGGS EPLVTVTVQC AFTVALRARR GADLSSLRAL LGQALPHQAQ LGQLSYLAPG
EDGHWVPIPE EESLQRAWQD AAACPRGLQL QCRGAGGRPV LYQVVAQHSY SAQGPEDLGF
RQGDTVDVLC EVDQAWLEGH CDGRIGIFPK CFVVPAGPRM SGAPGRLPRS QQGDQP


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CSB-EL015963RA Rat NADPH oxidase activator 1(NOXA1) ELISA kit SpeciesRat 96T
EIAAB27578 NADPH oxidase activator 1,Noxa1,Rat,Rattus norvegicus
CSB-EL015963MO Mouse NADPH oxidase activator 1(NOXA1) ELISA kit SpeciesMouse 96T
NOXA1_RAT ELISA Kit FOR NADPH oxidase activator 1; organism: Rat; gene name: Noxa1 96T
CSB-EL015963HU Human NADPH oxidase activator 1(NOXA1) ELISA kit SpeciesHuman 96T
NOXA1_MOUSE ELISA Kit FOR NADPH oxidase activator 1; organism: Mouse; gene name: Noxa1 96T
EIAAB41248 Ccdc44,Coiled-coil domain-containing protein 44,Mouse,Mus musculus,Taco1,Translational activator of cytochrome c oxidase 1,Translational activator of mitochondrially-encoded cytochrome c oxidase 1
EIAAB26523 Ncf2,NCF-2,Neutrophil cytosol factor 2,Neutrophil NADPH oxidase factor 2,Rat,Rattus norvegicus
CSB-EL015963RA Rat NADPH oxidase activator 1 (NOXA1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB37274 Cerebroside sulfate activator protein,Ganglioside GM2 activator,GM2A,GM2-AP,Homo sapiens,Human,SAP-3,Shingolipid activator protein 3
EIAAB37275 Cerebroside sulfate activator protein,Ganglioside GM2 activator,Gm2a,GM2-AP,Mouse,Mus musculus,SAP-3,Shingolipid activator protein 3
EIAAB11719 Dual oxidase activator 1,Dual oxidase maturation factor 1,DUOXA1,Homo sapiens,Human,NIP,Numb-interacting protein,NUMBIP


 

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