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

Cytochrome b-245 light chain (Cytochrome b(558) alpha chain) (Cytochrome b558 subunit alpha) (Neutrophil cytochrome b 22 kDa polypeptide) (Superoxide-generating NADPH oxidase light chain subunit) (p22 phagocyte B-cytochrome) (p22-phox) (p22phox)

 CY24A_MOUSE             Reviewed;         192 AA.
Q61462; Q3U820; Q9CWB9; Q9D2W2;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-DEC-2017, entry version 148.
RecName: Full=Cytochrome b-245 light chain;
AltName: Full=Cytochrome b(558) alpha chain;
AltName: Full=Cytochrome b558 subunit alpha;
AltName: Full=Neutrophil cytochrome b 22 kDa polypeptide;
AltName: Full=Superoxide-generating NADPH oxidase light chain subunit;
AltName: Full=p22 phagocyte B-cytochrome;
AltName: Full=p22-phox;
Short=p22phox;
Name=Cyba;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-192 (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Macrophage;
PubMed=2597164; DOI=10.1016/S0006-291X(89)80051-8;
Sumimoto H., Nozaki M., Sasaki H., Takeshige K., Sakaki Y.,
Minakami S.;
"Complementary DNA for the mouse homolog of the small subunit of human
cytochrome b558.";
Biochem. Biophys. Res. Commun. 165:902-906(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryonic stem cell, and Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-176, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[5]
FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH SH3PXD2A.
PubMed=19755709; DOI=10.1126/scisignal.2000368;
Diaz B., Shani G., Pass I., Anderson D., Quintavalle M.,
Courtneidge S.A.;
"Tks5-dependent, nox-mediated generation of reactive oxygen species is
necessary for invadopodia formation.";
Sci. Signal. 2:RA53-RA53(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-176, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Critical component of the membrane-bound oxidase of
phagocytes that generates superoxide. Associates with NOX3 to form
a functional NADPH oxidase constitutively generating superoxide.
{ECO:0000269|PubMed:19755709}.
-!- SUBUNIT: Composed of a heavy chain (beta) and a light chain
(alpha). 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 with NCF1 (via
SH3 domain). Interacts with DUOX1, DUOX2 and TPO. Interacts with
NOX3 and NOX4. Interacts with calprotectin (S100A8/9) (By
similarity). Interacts with SH3PXD2A. {ECO:0000250,
ECO:0000269|PubMed:19755709}.
-!- INTERACTION:
Q61093:Cybb; NbExp=4; IntAct=EBI-15795776, EBI-6654585;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q61462-1; Sequence=Displayed;
Name=2;
IsoId=Q61462-2; Sequence=VSP_001248;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: The strongest level of expression is found in
kidney, peritoneal neutrophils and peritoneal macrophages, and a
lower level in spleen and small intestine. Very low level of
expression can be noted in brain, liver, testis, and heart.
{ECO:0000269|PubMed:2597164}.
-!- PTM: The heme prosthetic group could be coordinated with residues
of the light chain, the heavy chain, or both, and it is possible
that more than one heme is present per cytochrome b-245.
{ECO:0000250}.
-!- PTM: Phosphorylation at Thr-147 enhances NADPH oxidase activity by
promoting p47phox binding. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show defects in invadopodia biogenesis.
{ECO:0000269|PubMed:19755709}.
-!- SIMILARITY: Belongs to the p22phox family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M31775; AAA37513.1; -; mRNA.
EMBL; AK018713; BAB31361.1; -; mRNA.
EMBL; AK021200; BAB32327.1; -; mRNA.
EMBL; AK152414; BAE31199.1; -; mRNA.
EMBL; BC026791; AAH26791.1; -; mRNA.
CCDS; CCDS22737.1; -. [Q61462-1]
CCDS; CCDS85623.1; -. [Q61462-2]
PIR; A36747; A36747.
RefSeq; NP_001288213.1; NM_001301284.1. [Q61462-2]
RefSeq; NP_031832.2; NM_007806.3. [Q61462-1]
UniGene; Mm.271671; -.
SMR; Q61462; -.
BioGrid; 198989; 1.
DIP; DIP-60456N; -.
IntAct; Q61462; 2.
STRING; 10090.ENSMUSP00000017604; -.
iPTMnet; Q61462; -.
PhosphoSitePlus; Q61462; -.
SwissPalm; Q61462; -.
PaxDb; Q61462; -.
PRIDE; Q61462; -.
Ensembl; ENSMUST00000017604; ENSMUSP00000017604; ENSMUSG00000006519. [Q61462-1]
Ensembl; ENSMUST00000212600; ENSMUSP00000148320; ENSMUSG00000006519. [Q61462-2]
GeneID; 13057; -.
KEGG; mmu:13057; -.
UCSC; uc009nsp.2; mouse. [Q61462-1]
UCSC; uc009nsq.2; mouse. [Q61462-2]
CTD; 1535; -.
MGI; MGI:1316658; Cyba.
eggNOG; ENOG410IXYN; Eukaryota.
eggNOG; ENOG4111MI6; LUCA.
GeneTree; ENSGT00390000002290; -.
HOGENOM; HOG000001585; -.
HOVERGEN; HBG051278; -.
InParanoid; Q61462; -.
KO; K08009; -.
OMA; EQWTPIE; -.
OrthoDB; EOG091G0NNC; -.
PhylomeDB; Q61462; -.
TreeFam; TF328901; -.
Reactome; R-MMU-1222556; ROS, RNS production in phagocytes.
Reactome; R-MMU-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:Q61462; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000006519; -.
CleanEx; MM_CYBA; -.
ExpressionAtlas; Q61462; baseline and differential.
Genevisible; Q61462; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043020; C:NADPH oxidase complex; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:Ensembl.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0009055; F:electron transfer activity; ISO:MGI.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; IBA:GO_Central.
GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:1904845; P:cellular response to L-glutamine; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0017004; P:cytochrome complex assembly; ISO:MGI.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; ISO:MGI.
GO; GO:0045087; P:innate immune response; ISO:MGI.
GO; GO:0003106; P:negative regulation of glomerular filtration by angiotensin; IEA:Ensembl.
GO; GO:0055114; P:oxidation-reduction process; ISO:MGI.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:1900426; P:positive regulation of defense response to bacterium; ISO:MGI.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
GO; GO:0070257; P:positive regulation of mucus secretion; IMP:MGI.
GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; IEA:Ensembl.
GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:MGI.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; ISO:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:MGI.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:MGI.
GO; GO:0045730; P:respiratory burst; ISO:MGI.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:1904044; P:response to aldosterone; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0014895; P:smooth muscle hypertrophy; IEA:Ensembl.
GO; GO:0042554; P:superoxide anion generation; ISO:MGI.
GO; GO:0006801; P:superoxide metabolic process; ISO:MGI.
InterPro; IPR007732; Cyt_b558_asu.
PANTHER; PTHR15168; PTHR15168; 1.
Pfam; PF05038; Cytochrom_B558a; 1.
PIRSF; PIRSF019635; Cytochr_b558a; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Electron transport; Heme; Iron; Membrane; Metal-binding; NADP;
Oxidoreductase; Phosphoprotein; Reference proteome; Transport.
CHAIN 1 192 Cytochrome b-245 light chain.
/FTId=PRO_0000144908.
INTRAMEM 91 127 {ECO:0000250}.
METAL 94 94 Iron (heme axial ligand). {ECO:0000255}.
MOD_RES 147 147 Phosphothreonine.
{ECO:0000250|UniProtKB:P13498}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 68 96 CGQKYLTSVVKLFGPLTRNYYVRAALHFL -> W (in
isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_001248.
CONFLICT 75 75 S -> P (in Ref. 2; BAB32327).
{ECO:0000305}.
SEQUENCE 192 AA; 20748 MW; 10DA1F9A54F44E80 CRC64;
MGQIEWAMWA NEQALASGLI LITGGIVATA GRFTQWYFGA YSIAAGVLIC LLEYPRGKRK
KGSTMERCGQ KYLTSVVKLF GPLTRNYYVR AALHFLLSVP AGFLLATILG TVCLAIASVI
YLLAAIRGEQ WTPIEPKPKE RPQVGGTIKQ PPTNPPPRPP AEVRKKPSEG EEEAASAGGP
QVNPMPVTDE VV


Related products :

Catalog number Product name Quantity
EIAAB10222 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,Pig,Superoxide-gene
EIAAB10220 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Homo sapiens,Human,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,
EIAAB10221 Bos taurus,Bovine,CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,S
EIAAB10219 Cyba,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Mouse,Mus musculus,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,
EIAAB10224 Cyba,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,Rat,Rattus norvegic
EIAAB10223 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,Oryctolagus cuniculus,p22 phagocyte B-cytochrome,p22phox,p22-ph
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
EIAAB10228 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,Neutrophil cytochrome b 91 kDa pol
EIAAB10227 Cgd,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,Mouse,Mus musculus,Neutrophil
EIAAB10226 Bos taurus,Bovine,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,Neutrophil cytoc
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
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
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
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
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
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
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
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
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
EIAAB10080 Bos taurus,Bovine,COX6A1,Cytochrome c oxidase polypeptide VIa-liver,Cytochrome c oxidase subunit 6A1, mitochondrial,Cytochrome c oxidase subunit SSG
EIAAB08773 Cox7c,Cox7c1,Cytochrome c oxidase polypeptide VIIc,Cytochrome c oxidase polypeptide VIIIA,Cytochrome c oxidase subunit 7C, mitochondrial,Rat,Rattus norvegicus
EIAAB10087 Bos taurus,Bovine,COX6A,COX6A2,COXVIAH,Cytochrome c oxidase polypeptide VIa-heart,Cytochrome c oxidase polypeptide VIb,Cytochrome c oxidase subunit 6A2, mitochondrial


 

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