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

Peroxiredoxin-4 (EC 1.11.1.15) (Antioxidant enzyme AOE372) (Peroxiredoxin IV) (Prx-IV) (Thioredoxin peroxidase AO372) (Thioredoxin-dependent peroxide reductase A0372)

 PRDX4_MOUSE             Reviewed;         274 AA.
O08807; B1AZS7; Q3U8E4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
25-OCT-2017, entry version 160.
RecName: Full=Peroxiredoxin-4;
EC=1.11.1.15;
AltName: Full=Antioxidant enzyme AOE372;
AltName: Full=Peroxiredoxin IV;
Short=Prx-IV;
AltName: Full=Thioredoxin peroxidase AO372;
AltName: Full=Thioredoxin-dependent peroxide reductase A0372;
Flags: Precursor;
Name=Prdx4;
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], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=C57BL/6J;
PubMed=11229364; DOI=10.1089/15230860050192288;
Wong C.M., Chun A.C., Kok K.H., Zhou Y., Fung P.C., Kung H.F.,
Jeang K.-T., Jin D.-Y.;
"Characterization of human and mouse peroxiredoxin IV: evidence for
inhibition by Prx-IV of epidermal growth factor- and p53-induced
reactive oxygen species.";
Antioxid. Redox Signal. 2:507-518(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2J; TISSUE=Bone marrow, and Liver;
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 GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NMRI; TISSUE=Mammary gland, and Mammary tumor;
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).
[5]
PROTEIN SEQUENCE OF 190-203 AND 216-226.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[7]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND DISULFIDE BONDS.
PubMed=23949117; DOI=10.1038/srep02456;
Sato Y., Kojima R., Okumura M., Hagiwara M., Masui S., Maegawa K.,
Saiki M., Horibe T., Suzuki M., Inaba K.;
"Synergistic cooperation of PDI family members in peroxiredoxin 4-
driven oxidative protein folding.";
Sci. Rep. 3:2456-2456(2013).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events (PubMed:11229364).
Regulates the activation of NF-kappa-B in the cytosol by a
modulation of I-kappa-B-alpha phosphorylation (By similarity).
{ECO:0000250|UniProtKB:Q13162, ECO:0000269|PubMed:11229364}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000250|UniProtKB:Q13162}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
assemble to form a ring-like decamer.
{ECO:0000250|UniProtKB:Q13162}.
-!- INTERACTION:
Q8NBS9-1:TXNDC5 (xeno); NbExp=2; IntAct=EBI-494652, EBI-16091651;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13162}.
Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13162}. Note=Not
secreted. {ECO:0000269|PubMed:11229364}.
-!- PTM: The enzyme can be inactivated by further oxidation of the
cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H)
and sulphonic acid (C(P)-SO3H) instead of its condensation to a
disulfide bond. {ECO:0000250|UniProtKB:Q13162}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by
the other dimeric subunit to form an intersubunit disulfide. The
disulfide is subsequently reduced by thioredoxin.
{ECO:0000250|UniProtKB:Q13162}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U96746; AAB57846.1; -; mRNA.
EMBL; AK005031; BAB23758.1; -; mRNA.
EMBL; AK146402; BAE27143.1; -; mRNA.
EMBL; AK152255; BAE31074.1; -; mRNA.
EMBL; BX005263; CAM23139.1; -; Genomic_DNA.
EMBL; BC003349; AAH03349.1; -; mRNA.
EMBL; BC019578; AAH19578.1; -; mRNA.
CCDS; CCDS30496.1; -.
RefSeq; NP_001300640.1; NM_001313711.1.
RefSeq; NP_058044.1; NM_016764.5.
UniGene; Mm.247542; -.
PDB; 3VWU; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J=41-274.
PDB; 3VWV; X-ray; 1.80 A; A/B=87-274.
PDB; 3W8J; X-ray; 2.10 A; C/D=244-263.
PDB; 3WGX; X-ray; 0.92 A; C/D=244-263.
PDBsum; 3VWU; -.
PDBsum; 3VWV; -.
PDBsum; 3W8J; -.
PDBsum; 3WGX; -.
ProteinModelPortal; O08807; -.
SMR; O08807; -.
BioGrid; 207303; 2.
DIP; DIP-34137N; -.
IntAct; O08807; 8.
MINT; MINT-1862981; -.
STRING; 10090.ENSMUSP00000026328; -.
PeroxiBase; 4532; Mm2CysPrx04.
iPTMnet; O08807; -.
PhosphoSitePlus; O08807; -.
SwissPalm; O08807; -.
REPRODUCTION-2DPAGE; O08807; -.
EPD; O08807; -.
MaxQB; O08807; -.
PaxDb; O08807; -.
PeptideAtlas; O08807; -.
PRIDE; O08807; -.
Ensembl; ENSMUST00000026328; ENSMUSP00000026328; ENSMUSG00000025289.
GeneID; 53381; -.
KEGG; mmu:53381; -.
UCSC; uc009uru.1; mouse.
CTD; 10549; -.
MGI; MGI:1859815; Prdx4.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00390000004653; -.
HOGENOM; HOG000022343; -.
HOVERGEN; HBG000286; -.
InParanoid; O08807; -.
KO; K03386; -.
OrthoDB; EOG091G0IE5; -.
PhylomeDB; O08807; -.
TreeFam; TF105181; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:O08807; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000025289; -.
CleanEx; MM_PRDX4; -.
ExpressionAtlas; O08807; baseline and differential.
Genevisible; O08807; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0019471; P:4-hydroxyproline metabolic process; IGI:MGI.
GO; GO:0045454; P:cell redox homeostasis; IGI:MGI.
GO; GO:0030198; P:extracellular matrix organization; IGI:MGI.
GO; GO:0008584; P:male gonad development; IMP:MGI.
GO; GO:2000255; P:negative regulation of male germ cell proliferation; IMP:MGI.
GO; GO:0055114; P:oxidation-reduction process; IMP:MGI.
GO; GO:0022417; P:protein maturation by protein folding; IGI:MGI.
GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Antioxidant; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Oxidoreductase; Peroxidase; Redox-active center; Reference proteome;
Signal.
SIGNAL 1 40 {ECO:0000250}.
CHAIN 41 274 Peroxiredoxin-4.
/FTId=PRO_0000135099.
DOMAIN 82 240 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 127 127 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:Q13162}.
MOD_RES 102 102 N6-succinyllysine.
{ECO:0000250|UniProtKB:P20108}.
DISULFID 127 127 Interchain (with C-248); in linked form.
{ECO:0000244|PDB:3VWU,
ECO:0000244|PDB:3VWV,
ECO:0000269|PubMed:23949117}.
DISULFID 248 248 Interchain (with C-127); in linked form.
{ECO:0000244|PDB:3VWU,
ECO:0000244|PDB:3VWV,
ECO:0000269|PubMed:23949117}.
STRAND 92 97 {ECO:0000244|PDB:3VWV}.
STRAND 100 105 {ECO:0000244|PDB:3VWV}.
HELIX 106 109 {ECO:0000244|PDB:3VWV}.
STRAND 112 118 {ECO:0000244|PDB:3VWV}.
STRAND 122 126 {ECO:0000244|PDB:3VWV}.
HELIX 129 136 {ECO:0000244|PDB:3VWV}.
HELIX 138 143 {ECO:0000244|PDB:3VWV}.
STRAND 146 154 {ECO:0000244|PDB:3VWV}.
HELIX 156 163 {ECO:0000244|PDB:3VWV}.
HELIX 167 169 {ECO:0000244|PDB:3VWV}.
STRAND 179 181 {ECO:0000244|PDB:3VWV}.
HELIX 186 190 {ECO:0000244|PDB:3VWV}.
TURN 196 199 {ECO:0000244|PDB:3VWV}.
STRAND 204 208 {ECO:0000244|PDB:3VWV}.
STRAND 212 219 {ECO:0000244|PDB:3VWV}.
HELIX 226 244 {ECO:0000244|PDB:3VWV}.
SEQUENCE 274 AA; 31053 MW; 73DB5374EC46241C CRC64;
MEARSKLLDG TTASRRWTRK LVLLLPPLLL FLLRTESLQG LESDERFRTR ENECHFYAGG
QVYPGEASRV SVADHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP
LDFTFVCPTE IIAFGDRIEE FKSINTEVVA CSVDSQFTHL AWINTPRRQG GLGPIRIPLL
SDLNHQISKD YGVYLEDSGH TLRGLFIIDD KGVLRQITLN DLPVGRSVDE TLRLVQAFQY
TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN


Related products :

Catalog number Product name Quantity
EIAAB32327 Antioxidant enzyme AOE372,Mouse,Mus musculus,Peroxiredoxin IV,Peroxiredoxin-4,Prdx4,Prx-IV,Thioredoxin peroxidase AO372,Thioredoxin-dependent peroxide reductase A0372
EIAAB32326 Antioxidant enzyme AOE372,Peroxiredoxin IV,Peroxiredoxin-4,Prdx4,Prx-IV,Rat,Rattus norvegicus,Rno2CysPrx04,Thioredoxin peroxidase AO372,Thioredoxin-dependent peroxide reductase A0372
EIAAB32329 Antioxidant enzyme AOE372,AOE37-2,Homo sapiens,Human,Peroxiredoxin IV,Peroxiredoxin-4,PRDX4,Prx-IV,Thioredoxin peroxidase AO372,Thioredoxin-dependent peroxide reductase A0372
E1123p ELISA kit Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123p ELISA Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
U1123p CLIA Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123m ELISA Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 96T
U1123r CLIA Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123r ELISA kit Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123r ELISA Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
U1123m CLIA Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 96T
E1123m ELISA kit Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 96T
15-288-21018 Peroxiredoxin-2 - EC 1.11.1.15; Thioredoxin peroxidase 1; Thioredoxin-dependent peroxide reductase 1; Thiol-specific antioxidant protein; TSA; PRP; Natural killer cell-enhancing factor B; NKEF-B Polyc 0.1 mg
15-288-21018 Peroxiredoxin-2 - EC 1.11.1.15; Thioredoxin peroxidase 1; Thioredoxin-dependent peroxide reductase 1; Thiol-specific antioxidant protein; TSA; PRP; Natural killer cell-enhancing factor B; NKEF-B Polyc 0.05 mg
E0703r ELISA Antioxidant enzyme B166,AOEB166,Peroxiredoxin V,Peroxiredoxin-5, mitochondrial,Peroxisomal antioxidant enzyme,PLP,Prdx5,Prx-V,Rat,Rattus norvegicus,Thioredoxin peroxidase PMP20,Thioredoxin reduc 96T
U0703r CLIA Antioxidant enzyme B166,AOEB166,Peroxiredoxin V,Peroxiredoxin-5, mitochondrial,Peroxisomal antioxidant enzyme,PLP,Prdx5,Prx-V,Rat,Rattus norvegicus,Thioredoxin peroxidase PMP20,Thioredoxin reduct 96T
E0703r ELISA kit Antioxidant enzyme B166,AOEB166,Peroxiredoxin V,Peroxiredoxin-5, mitochondrial,Peroxisomal antioxidant enzyme,PLP,Prdx5,Prx-V,Rat,Rattus norvegicus,Thioredoxin peroxidase PMP20,Thioredoxin 96T
E2222r HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2
EIAAB32322 Antioxidant protein 1,AOP1,AOP-1,HBC189,Homo sapiens,Human,Peroxiredoxin III,Peroxiredoxin-3,PRDX3,Protein MER5 homolog,Prx-III,Thioredoxin-dependent peroxide reductase, mitochondrial
E2222r ELISA kit HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
U2222r CLIA HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
E2222r ELISA HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
U2222r CLIA kit HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
E1123h ELISA Homo sapiens,Human,Natural killer cell-enhancing factor B,NKEFB,NKEF-B,Peroxiredoxin-2,PRDX2,PRP,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide 96T
U1123h CLIA Homo sapiens,Human,Natural killer cell-enhancing factor B,NKEFB,NKEF-B,Peroxiredoxin-2,PRDX2,PRP,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide r 96T


 

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