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Neutrophil cytosol factor 1 (NCF-1) (47 kDa autosomal chronic granulomatous disease protein) (47 kDa neutrophil oxidase factor) (NCF-47K) (Neutrophil NADPH oxidase factor 1) (Nox organizer 2) (Nox-organizing protein 2) (SH3 and PX domain-containing protein 1A) (p47-phox)

 NCF1_HUMAN              Reviewed;         390 AA.
P14598; A6NEH2; A8K7S9; O43842; Q2PP07; Q53FR5; Q9BU90; Q9BXI7;
Q9BXI8; Q9UDV9; Q9UMU2;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
08-MAR-2011, sequence version 3.
22-NOV-2017, entry version 212.
RecName: Full=Neutrophil cytosol factor 1;
Short=NCF-1;
AltName: Full=47 kDa autosomal chronic granulomatous disease protein;
AltName: Full=47 kDa neutrophil oxidase factor;
AltName: Full=NCF-47K;
AltName: Full=Neutrophil NADPH oxidase factor 1;
AltName: Full=Nox organizer 2;
AltName: Full=Nox-organizing protein 2;
AltName: Full=SH3 and PX domain-containing protein 1A;
AltName: Full=p47-phox;
Name=NCF1; Synonyms=NOXO2, SH3PXD1A;
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), FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=2550933; DOI=10.1073/pnas.86.18.7195;
Volpp B.D., Nauseef W.M., Clark R.A.;
"Cloning of the cDNA and functional expression of the 47-kilodalton
cytosolic component of human neutrophil respiratory burst oxidase.";
Proc. Natl. Acad. Sci. U.S.A. 86:7195-7199(1989).
[2]
ERRATUM, AND SEQUENCE REVISION.
Volpp B.D., Nauseef W.M., Clark R.A.;
Proc. Natl. Acad. Sci. U.S.A. 86:9563-9563(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND VARIANTS SER-99 AND ASP-166.
PubMed=2547247; DOI=10.1126/science.2547247;
Lomax K.J., Leto T.L., Nunoi H., Gallin J.I., Malech H.L.;
"Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in
chronic granulomatous disease.";
Science 245:409-412(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-99 AND
ASP-166.
PubMed=2398896; DOI=10.1128/MCB.10.10.5388;
Rodaway A.R.F., Teahan C.G., Casimir C.M., Segal A.W., Bentley D.L.;
"Characterization of the 47-kilodalton autosomal chronic granulomatous
disease protein: tissue-specific expression and transcriptional
control by retinoic acid.";
Mol. Cell. Biol. 10:5388-5396(1990).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-99.
PubMed=9329953; DOI=10.1172/JCI119721;
Gorlach A., Lee P.L., Roesler J., Hopkins P.J., Christensen B.,
Green E.D., Chanock S.J., Curnutte J.T.;
"A p47-phox pseudogene carries the most common mutation causing p47-
phox-deficient chronic granulomatous disease.";
J. Clin. Invest. 100:1907-1918(1997).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-99.
PubMed=10772875; DOI=10.1006/bcmd.2000.0274;
Chanock S.J., Roesler J., Zhan S., Hopkins P., Lee P., Barrett D.T.,
Christensen B.L., Curnutte J.T., Goerlach A.;
"Genomic structure of the human p47-phox (NCF1) gene.";
Blood Cells Mol. Dis. 26:37-46(2000).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-99; ASP-166
AND GLU-258.
TISSUE=Umbilical vein;
PubMed=11740866; DOI=10.1006/excr.2001.5404;
Gu Y., Xu Y.C., Wu R.F., Souza R.F., Nwariaku F.E., Terada L.S.;
"TNFalpha activates c-jun amino terminal kinase through p47(phox).";
Exp. Cell Res. 272:62-74(2002).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
SER-99.
TISSUE=Spleen, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-99.
TISSUE=Spleen;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-99.
TISSUE=Lymph;
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).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-31 (ISOFORM 1).
TISSUE=Ovary;
PubMed=7581362; DOI=10.1093/hmg/4.8.1259;
Harshman K., Bell R., Rosenthal J., Katcher H., Miki Y., Swenson J.,
Gholami Z., Frye C., Ding W., Dayananth P., Eddington K., Norris F.H.,
Bristow P.K., Phelps R., Hattier T., Stone S., Shaffer D., Bayer S.,
Hussey C., Tran T., Lai M., Rosteck P.R. Jr., Skolnick M.H.,
Shattuck-Eidens D., Kamb A.;
"Comparison of the positional cloning methods used to isolate the
BRCA1 gene.";
Hum. Mol. Genet. 4:1259-1266(1995).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-24, AND INVOLVEMENT IN CHRONIC
GRANULOMATOUS DISEASE.
PubMed=2011585; DOI=10.1073/pnas.88.7.2753;
Casimir C.M., Bu-Ghanim H.N., Rodaway A.R., Bentley D.L., Rowe P.,
Segal A.W.;
"Autosomal recessive chronic granulomatous disease caused by deletion
at a dinucleotide repeat.";
Proc. Natl. Acad. Sci. U.S.A. 88:2753-2757(1991).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-390, AND VARIANT ASP-166.
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[15]
PHOSPHORYLATION AT SER-303; SER-304; SER-320; SER-328; SER-345 AND
SER-348.
PubMed=8089108;
el Benna J., Faust L.P., Babior B.M.;
"The phosphorylation of the respiratory burst oxidase component
p47phox during neutrophil activation. Phosphorylation of sites
recognized by protein kinase C and by proline-directed kinases.";
J. Biol. Chem. 269:23431-23436(1994).
[16]
INTERACTION WITH CYBB.
PubMed=9224653; DOI=10.1042/bj3250249;
Adams E.R., Dratz E.A., Gizachew D., Deleo F.R., Yu L., Volpp B.D.,
Vlases M., Jesaitis A.J., Quinn M.T.;
"Interaction of human neutrophil flavocytochrome b with cytosolic
proteins: transferred-NOESY NMR studies of a gp91phox C-terminal
peptide bound to p47phox.";
Biochem. J. 325:249-257(1997).
[17]
INTERACTION WITH TRAF4, AND SUBCELLULAR LOCATION.
PubMed=12023963; DOI=10.1074/jbc.M202665200;
Xu Y.C., Wu R.F., Gu Y., Yang Y.S., Yang M.C., Nwariaku F.E.,
Terada L.S.;
"Involvement of TRAF4 in oxidative activation of c-Jun N-terminal
kinase.";
J. Biol. Chem. 277:28051-28057(2002).
[18]
INTERACTION WITH NOXA1.
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).
[19]
INTERACTION WITH TRAF4.
PubMed=16052631; DOI=10.1002/eji.200526151;
Takeshita F., Ishii K.J., Kobiyama K., Kojima Y., Coban C., Sasaki S.,
Ishii N., Klinman D.M., Okuda K., Akira S., Suzuki K.;
"TRAF4 acts as a silencer in TLR-mediated signaling through the
association with TRAF6 and TRIF.";
Eur. J. Immunol. 35:2477-2485(2005).
[20]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[21]
INTERACTION WITH ADAM15.
PubMed=19718658; DOI=10.1002/jcb.22317;
Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.;
"Alternative splicing of ADAM15 regulates its interactions with
cellular SH3 proteins.";
J. Cell. Biochem. 108:877-885(2009).
[22]
FUNCTION, AND PHOSPHORYLATION.
PubMed=19801500; DOI=10.1189/jlb.0408230;
Kilpatrick L.E., Sun S., Li H., Vary T.C., Korchak H.M.;
"Regulation of TNF-induced oxygen radical production in human
neutrophils: role of delta-PKC.";
J. Leukoc. Biol. 87:153-164(2010).
[23]
STRUCTURE BY NMR OF 1-128.
PubMed=11373621; DOI=10.1038/88591;
Hiroaki H., Ago T., Ito T., Sumimoto H., Kohda D.;
"Solution structure of the PX domain, a target of the SH3 domain.";
Nat. Struct. Biol. 8:526-530(2001).
[24]
STRUCTURE BY NMR OF 359-390 IN COMPLEX WITH NCF2, AND INTERACTION WITH
NCF2.
PubMed=12169629; DOI=10.1093/emboj/cdf428;
Kami K., Takeya R., Sumimoto H., Kohda D.;
"Diverse recognition of non-PxxP peptide ligands by the SH3 domains
from p67(phox), Grb2 and Pex13p.";
EMBO J. 21:4268-4276(2002).
[25]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-123, DOMAIN,
LIPID-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-43;
TRP-263; SER-303; SER-304; SER-328; SER-359 AND SER-370.
PubMed=12356722; DOI=10.1093/emboj/cdf519;
Karathanassis D., Stahelin R.V., Bravo J., Perisic O., Pacold C.M.,
Cho W., Williams R.L.;
"Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-
bisphosphate and phosphatidic acid is masked by an intramolecular
interaction.";
EMBO J. 21:5057-5068(2002).
[26]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 156-340, DOMAIN, AND
INTERACTION WITH CYBA.
PubMed=12732142; DOI=10.1016/S0092-8674(03)00314-3;
Groemping Y., Lapouge K., Smerdon S.J., Rittinger K.;
"Molecular basis of phosphorylation-induced activation of the NADPH
oxidase.";
Cell 113:343-355(2003).
[27]
X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 151-340.
PubMed=15147273; DOI=10.1111/j.1356-9597.2004.00733.x;
Yuzawa S., Suzuki N.N., Fujioka Y., Ogura K., Sumimoto H., Inagaki F.;
"A molecular mechanism for autoinhibition of the tandem SH3 domains of
p47phox, the regulatory subunit of the phagocyte NADPH oxidase.";
Genes Cells 9:443-456(2004).
[28]
X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 360-372 IN COMPLEX WITH
NCF4, AND SUBUNIT.
PubMed=15657040; DOI=10.1074/jbc.M412897200;
Massenet C., Chenavas S., Cohen-Addad C., Dagher M.-C., Brandolin G.,
Pebay-Peyroula E., Fieschi F.;
"Effects of p47phox C terminus phosphorylations on binding
interactions with p40phox and p67phox. Structural and functional
comparison of p40phox and p67phox SH3 domains.";
J. Biol. Chem. 280:13752-13761(2005).
[29]
STRUCTURE BY NMR OF 151-286 IN COMPLEX WITH CYBA, AND INTERACTION WITH
CYBA.
PubMed=16326715; DOI=10.1074/jbc.M505193200;
Ogura K., Nobuhisa I., Yuzawa S., Takeya R., Torikai S., Saikawa K.,
Sumimoto H., Inagaki F.;
"NMR solution structure of the tandem Src homology 3 domains of
p47phox complexed with a p22phox-derived proline-rich peptide.";
J. Biol. Chem. 281:3660-3668(2006).
[30]
INVOLVEMENT IN CGD1, VARIANT CGD1 GLN-42, AND VARIANT SER-262.
PubMed=11133775; DOI=10.1182/blood.V97.1.305;
Noack D., Rae J., Cross A.R., Ellis B.A., Newburger P.E.,
Curnutte J.T., Heyworth P.G.;
"Autosomal recessive chronic granulomatous disease caused by defects
in NCF1, the gene encoding the phagocyte p47-phox: mutations not
arising in the NCF1 pseudogenes.";
Blood 97:305-311(2001).
[31]
INVOLVEMENT IN CGD1.
PubMed=23910690; DOI=10.1016/j.jaci.2013.05.039;
Koeker M.Y., Camcioglu Y., van Leeuwen K., Kilic S.S., Barlan I.,
Yilmaz M., Metin A., de Boer M., Avcilar H., Patiroglu T.,
Yildiran A., Yegin O., Tezcan I., Sanal O., Roos D.;
"Clinical, functional, and genetic characterization of chronic
granulomatous disease in 89 Turkish patients.";
J. Allergy Clin. Immunol. 132:1156-1163(2013).
[32]
VARIANT HIS-90.
PubMed=28135245; DOI=10.1038/ng.3782;
Zhao J., Ma J., Deng Y., Kelly J.A., Kim K., Bang S.Y., Lee H.S.,
Li Q.Z., Wakeland E.K., Qiu R., Liu M., Guo J., Li Z., Tan W.,
Rasmussen A., Lessard C.J., Sivils K.L., Hahn B.H., Grossman J.M.,
Kamen D.L., Gilkeson G.S., Bae S.C., Gaffney P.M., Shen N., Tsao B.P.;
"A missense variant in NCF1 is associated with susceptibility to
multiple autoimmune diseases.";
Nat. Genet. 49:433-437(2017).
-!- FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are
required for activation of the latent NADPH oxidase (necessary for
superoxide production). {ECO:0000269|PubMed:19801500,
ECO:0000269|PubMed:2547247, ECO:0000269|PubMed:2550933}.
-!- SUBUNIT: Component of an NADPH oxidase complex composed of a
heterodimer formed by the membrane proteins CYBA and CYBB and the
cytosolic subunits NCF1, NCF2 and NCF4. Interacts (via C-terminus)
with NCF2 (via the C-terminal SH3 domain). Interacts with NCF4.
Interacts with CYBB. Interacts (via the second SH3 domain) with
CYBA. Interacts with NOXA1. Interacts with ADAM15. Interacts with
TRAF4. Interacts with FASLG. Interacts with PARK7 (via C-
terminus); the interaction is enhanced by LPS and modulates NCF1
phosphorylation and membrane translocation (By similarity).
{ECO:0000250|UniProtKB:Q09014, ECO:0000269|PubMed:12023963,
ECO:0000269|PubMed:12169629, ECO:0000269|PubMed:12716910,
ECO:0000269|PubMed:12732142, ECO:0000269|PubMed:15657040,
ECO:0000269|PubMed:16052631, ECO:0000269|PubMed:16326715,
ECO:0000269|PubMed:19718658, ECO:0000269|PubMed:19807924,
ECO:0000269|PubMed:2550933, ECO:0000269|PubMed:9224653}.
-!- INTERACTION:
Q8IZP0:ABI1; NbExp=5; IntAct=EBI-395044, EBI-375446;
P60709:ACTB; NbExp=3; IntAct=EBI-395044, EBI-353944;
P13498:CYBA; NbExp=7; IntAct=EBI-395044, EBI-986058;
P04899:GNAI2; NbExp=2; IntAct=EBI-395044, EBI-353997;
P11142:HSPA8; NbExp=2; IntAct=EBI-395044, EBI-351896;
P19878:NCF2; NbExp=13; IntAct=EBI-395044, EBI-489611;
Q15080:NCF4; NbExp=2; IntAct=EBI-395044, EBI-1036870;
Q05513:PRKCZ; NbExp=3; IntAct=EBI-395044, EBI-295351;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:2550933}. Membrane
{ECO:0000269|PubMed:12356722}; Peripheral membrane protein
{ECO:0000269|PubMed:12356722}; Cytoplasmic side
{ECO:0000269|PubMed:12356722}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P14598-1; Sequence=Displayed;
Name=2;
IsoId=P14598-2; Sequence=VSP_035032, VSP_035033;
Note=Due to intron retention.;
-!- TISSUE SPECIFICITY: Detected in peripheral blood monocytes and
neutrophils (at protein level). {ECO:0000269|PubMed:2547247,
ECO:0000269|PubMed:2550933}.
-!- DOMAIN: The PX domain mediates interaction with
phosphatidylinositol 3,4-bisphosphate and other anionic
phospholipids. In the autoinhibited, unphosphorylated state an
intramolecular interaction with the C-terminal SH3 domain
precludes phospholipid binding and interaction with CYBA.
Phosphorylation disrupts the autoinhibited state.
{ECO:0000269|PubMed:12356722, ECO:0000269|PubMed:12732142}.
-!- PTM: Phosphorylated by PRKCD; phosphorylation induces activation
of NCF1 and NADPH oxidase activity. {ECO:0000269|PubMed:19801500,
ECO:0000269|PubMed:8089108}.
-!- DISEASE: Granulomatous disease, chronic, cytochrome-b-positive 1,
autosomal recessive (CGD1) [MIM:233700]: A disorder characterized
by the inability of neutrophils and phagocytes to kill microbes
that they have ingested. Patients suffer from life-threatening
bacterial/fungal infections. {ECO:0000269|PubMed:11133775,
ECO:0000269|PubMed:23910690}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAF84783.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG54596.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NCF1base; Note=NCF1 deficiency database;
URL="http://structure.bmc.lu.se/idbase/NCF1base/";
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EMBL; M25665; AAA57209.1; -; mRNA.
EMBL; M55067; AAA59901.1; -; mRNA.
EMBL; U57835; AAB95193.1; -; Genomic_DNA.
EMBL; U57833; AAB95193.1; JOINED; Genomic_DNA.
EMBL; U57834; AAB95193.1; JOINED; Genomic_DNA.
EMBL; AF184614; AAF34737.1; -; Genomic_DNA.
EMBL; AF330625; AAK19516.1; -; mRNA.
EMBL; AF330626; AAK19517.1; -; mRNA.
EMBL; AF330627; AAK19518.1; -; mRNA.
EMBL; AK127905; BAG54596.1; ALT_INIT; mRNA.
EMBL; AK292094; BAF84783.1; ALT_INIT; mRNA.
EMBL; AK223217; BAD96937.1; -; mRNA.
EMBL; AC004883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC083884; AAS07465.1; -; Genomic_DNA.
EMBL; AC124781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002816; AAH02816.1; -; mRNA.
EMBL; BC065731; AAH65731.1; -; mRNA.
EMBL; U25793; AAA93232.1; -; mRNA.
EMBL; DQ314878; ABC40737.1; -; Genomic_DNA.
CCDS; CCDS34657.1; -. [P14598-1]
PIR; A35926; A39249.
RefSeq; NP_000256.4; NM_000265.5.
UniGene; Hs.647047; -.
UniGene; Hs.648940; -.
UniGene; Hs.655201; -.
PDB; 1GD5; NMR; -; A=1-128.
PDB; 1K4U; NMR; -; P=359-390.
PDB; 1KQ6; X-ray; 1.18 A; A=1-141.
PDB; 1NG2; X-ray; 1.70 A; A=156-340.
PDB; 1O7K; X-ray; 2.00 A; A/B/C=1-123.
PDB; 1OV3; X-ray; 1.80 A; A/B=156-285.
PDB; 1UEC; X-ray; 1.82 A; A=151-340.
PDB; 1W70; X-ray; 1.46 A; C/D=360-372.
PDB; 1WLP; NMR; -; B=151-286.
PDBsum; 1GD5; -.
PDBsum; 1K4U; -.
PDBsum; 1KQ6; -.
PDBsum; 1NG2; -.
PDBsum; 1O7K; -.
PDBsum; 1OV3; -.
PDBsum; 1UEC; -.
PDBsum; 1W70; -.
PDBsum; 1WLP; -.
ProteinModelPortal; P14598; -.
SMR; P14598; -.
BioGrid; 575724; 39.
DIP; DIP-126N; -.
ELM; P14598; -.
IntAct; P14598; 17.
MINT; MINT-139338; -.
STRING; 9606.ENSP00000289473; -.
BindingDB; P14598; -.
DrugBank; DB00514; Dextromethorphan.
iPTMnet; P14598; -.
PhosphoSitePlus; P14598; -.
DMDM; 325511390; -.
EPD; P14598; -.
MaxQB; P14598; -.
PaxDb; P14598; -.
PeptideAtlas; P14598; -.
PRIDE; P14598; -.
DNASU; 653361; -.
Ensembl; ENST00000289473; ENSP00000289473; ENSG00000158517.
GeneID; 653361; -.
KEGG; hsa:653361; -.
UCSC; uc003ubb.5; human. [P14598-1]
CTD; 653361; -.
DisGeNET; 653361; -.
EuPathDB; HostDB:ENSG00000158517.13; -.
GeneCards; NCF1; -.
GeneReviews; NCF1; -.
H-InvDB; HIX0033553; -.
HGNC; HGNC:7660; NCF1.
HPA; CAB004524; -.
HPA; HPA047836; -.
HPA; HPA052095; -.
MalaCards; NCF1; -.
MIM; 233700; phenotype.
MIM; 608512; gene.
neXtProt; NX_P14598; -.
Orphanet; 379; Chronic granulomatous disease.
PharmGKB; PA31463; -.
eggNOG; ENOG410IRR3; Eukaryota.
eggNOG; ENOG410YYZE; LUCA.
HOVERGEN; HBG002055; -.
InParanoid; P14598; -.
KO; K08011; -.
OrthoDB; EOG091G0CBF; -.
PhylomeDB; P14598; -.
TreeFam; TF329347; -.
Reactome; R-HSA-1222556; ROS, RNS production in phagocytes.
Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
SIGNOR; P14598; -.
EvolutionaryTrace; P14598; -.
GeneWiki; Neutrophil_cytosolic_factor_1; -.
GenomeRNAi; 653361; -.
PRO; PR:P14598; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000158517; -.
ExpressionAtlas; P14598; baseline and differential.
Genevisible; P14598; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0043020; C:NADPH oxidase complex; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0032010; C:phagolysosome; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:CAFA.
GO; GO:0002102; C:podosome; IBA:GO_Central.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IBA:GO_Central.
GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; IMP:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; TAS:Reactome.
GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
GO; GO:0071276; P:cellular response to cadmium ion; IDA:CAFA.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:CAFA.
GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
GO; GO:0071800; P:podosome assembly; IBA:GO_Central.
GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IMP:CAFA.
GO; GO:0046330; P:positive regulation of JNK cascade; IMP:CAFA.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; IMP:CAFA.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:CAFA.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
GO; GO:0006612; P:protein targeting to membrane; IDA:UniProtKB.
GO; GO:0045730; P:respiratory burst; TAS:BHF-UCL.
GO; GO:0042554; P:superoxide anion generation; IMP:UniProtKB.
GO; GO:0006801; P:superoxide metabolic process; TAS:BHF-UCL.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd06887; PX_p47phox; 1.
CDD; cd12021; SH3_p47phox_1; 1.
CDD; cd12022; SH3_p47phox_2; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR015039; NADPH_oxidase_p47Phox_C.
InterPro; IPR035756; NCF1_SH3_1.
InterPro; IPR035757; NCF1_SH3_2.
InterPro; IPR032136; NECFESHC.
InterPro; IPR001655; P47PHOX.
InterPro; IPR001683; Phox.
InterPro; IPR036871; PX_dom_sf.
InterPro; IPR034909; PX_p47phox.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR15706:SF6; PTHR15706:SF6; 1.
Pfam; PF16621; NECFESHC; 1.
Pfam; PF08944; p47_phox_C; 1.
Pfam; PF00787; PX; 1.
Pfam; PF00018; SH3_1; 2.
PRINTS; PR00498; P47PHOX.
SMART; SM00312; PX; 1.
SMART; SM00326; SH3; 2.
SUPFAM; SSF50044; SSF50044; 2.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50195; PX; 1.
PROSITE; PS50002; SH3; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chronic granulomatous disease;
Complete proteome; Cytoplasm; Disease mutation; Lipid-binding;
Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
SH3 domain.
CHAIN 1 390 Neutrophil cytosol factor 1.
/FTId=PRO_0000096762.
DOMAIN 4 125 PX. {ECO:0000255|PROSITE-
ProRule:PRU00147}.
DOMAIN 156 215 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 226 285 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COMPBIAS 211 254 Asp/Glu-rich (highly acidic).
COMPBIAS 292 390 Arg/Lys-rich (highly basic).
MOD_RES 303 303 Phosphoserine.
{ECO:0000269|PubMed:8089108}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000269|PubMed:8089108}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000269|PubMed:8089108}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000269|PubMed:8089108}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000269|PubMed:8089108}.
MOD_RES 348 348 Phosphoserine.
{ECO:0000269|PubMed:8089108}.
VAR_SEQ 193 193 W -> QTSHLTGLLPLVLRNPQPQAPCQGSGSLAPGRTPAL
LGALNVLPTLWVAFCLSVHPVVAVGICAWQAGAGHVCVFCL
DGYGTVCSL (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_035032.
VAR_SEQ 194 390 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_035033.
VARIANT 42 42 R -> Q (in CGD1).
{ECO:0000269|PubMed:11133775}.
/FTId=VAR_012476.
VARIANT 90 90 R -> H (polymorphism; may influence
susceptibility to systemic lupus
erythematosus; dbSNP:rs13447).
{ECO:0000269|PubMed:28135245}.
/FTId=VAR_014735.
VARIANT 99 99 G -> S (in dbSNP:rs17856077).
{ECO:0000269|PubMed:10772875,
ECO:0000269|PubMed:11740866,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2398896,
ECO:0000269|PubMed:2547247,
ECO:0000269|PubMed:9329953,
ECO:0000269|Ref.9}.
/FTId=VAR_018479.
VARIANT 160 160 T -> S.
/FTId=VAR_012477.
VARIANT 166 166 N -> D. {ECO:0000269|PubMed:11740866,
ECO:0000269|PubMed:2398896,
ECO:0000269|PubMed:2547247,
ECO:0000269|Ref.14}.
/FTId=VAR_012478.
VARIANT 258 258 K -> E. {ECO:0000269|PubMed:11740866}.
/FTId=VAR_018476.
VARIANT 262 262 G -> S. {ECO:0000269|PubMed:11133775}.
/FTId=VAR_012479.
VARIANT 308 308 A -> V (in dbSNP:rs13739).
/FTId=VAR_012480.
MUTAGEN 43 43 R->Q: Reduces affinity for membranes
enriched in phosphatidylinositol 3,4-
bisphosphate.
{ECO:0000269|PubMed:12356722}.
MUTAGEN 90 90 R->A: Reduces affinity for membranes
enriched in phosphatidylinositol 3,4-
bisphosphate.
MUTAGEN 263 263 W->R: Abolishes autoinhibition and
promotes phospholipid binding.
{ECO:0000269|PubMed:12356722}.
MUTAGEN 303 303 S->E: Abolishes autoinhibition and
promotes phospholipid binding; when
associated with E-304; E-328; E-359 and
E-370. {ECO:0000269|PubMed:12356722}.
MUTAGEN 304 304 S->E: Abolishes autoinhibition and
promotes phospholipid binding; when
associated with E-303; E-328; E-359 and
E-370. {ECO:0000269|PubMed:12356722}.
MUTAGEN 328 328 S->E: Abolishes autoinhibition and
promotes phospholipid binding; when
associated with E-303; E-304; E-359 and
E-370. {ECO:0000269|PubMed:12356722}.
MUTAGEN 359 359 S->E: Abolishes autoinhibition and
promotes phospholipid binding; when
associated with E-303; E-304; E-328 and
E-370. {ECO:0000269|PubMed:12356722}.
MUTAGEN 370 370 S->E: Abolishes autoinhibition and
promotes phospholipid binding; when
associated with E-303; E-304; E-328 and
E-359. {ECO:0000269|PubMed:12356722}.
CONFLICT 200 200 A -> T (in Ref. 7; AAK19516).
{ECO:0000305}.
STRAND 6 17 {ECO:0000244|PDB:1KQ6}.
STRAND 19 21 {ECO:0000244|PDB:1KQ6}.
STRAND 23 32 {ECO:0000244|PDB:1KQ6}.
STRAND 37 42 {ECO:0000244|PDB:1KQ6}.
HELIX 44 57 {ECO:0000244|PDB:1KQ6}.
TURN 59 63 {ECO:0000244|PDB:1KQ6}.
HELIX 67 69 {ECO:0000244|PDB:1KQ6}.
HELIX 78 80 {ECO:0000244|PDB:1O7K}.
HELIX 84 101 {ECO:0000244|PDB:1KQ6}.
HELIX 106 109 {ECO:0000244|PDB:1KQ6}.
HELIX 112 118 {ECO:0000244|PDB:1KQ6}.
HELIX 122 125 {ECO:0000244|PDB:1KQ6}.
STRAND 137 140 {ECO:0000244|PDB:1KQ6}.
STRAND 153 155 {ECO:0000244|PDB:1WLP}.
STRAND 159 162 {ECO:0000244|PDB:1NG2}.
STRAND 171 174 {ECO:0000244|PDB:1WLP}.
STRAND 182 187 {ECO:0000244|PDB:1NG2}.
STRAND 195 198 {ECO:0000244|PDB:1NG2}.
STRAND 202 206 {ECO:0000244|PDB:1OV3}.
HELIX 207 209 {ECO:0000244|PDB:1NG2}.
STRAND 210 214 {ECO:0000244|PDB:1OV3}.
STRAND 229 235 {ECO:0000244|PDB:1NG2}.
STRAND 241 244 {ECO:0000244|PDB:1WLP}.
STRAND 252 257 {ECO:0000244|PDB:1NG2}.
STRAND 262 268 {ECO:0000244|PDB:1NG2}.
STRAND 271 276 {ECO:0000244|PDB:1NG2}.
HELIX 277 279 {ECO:0000244|PDB:1NG2}.
STRAND 280 282 {ECO:0000244|PDB:1NG2}.
HELIX 287 292 {ECO:0000244|PDB:1NG2}.
HELIX 302 304 {ECO:0000244|PDB:1NG2}.
HELIX 321 328 {ECO:0000244|PDB:1NG2}.
HELIX 371 376 {ECO:0000244|PDB:1K4U}.
HELIX 380 385 {ECO:0000244|PDB:1K4U}.
SEQUENCE 390 AA; 44652 MW; 5A0F9F0EF101D2DB CRC64;
MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI
EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCGT LMSLPTKISR CPHLLDFFKV
RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG
DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV
EGDEVSLLEG EAVEVIHKLL DGWWVIRKDD VTGYFPSMYL QKSGQDVSQA QRQIKRGAPP
RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK
PQPAVPPRPS ADLILNRCSE STKRKLASAV


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