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

Peroxiredoxin TSA2 (Prx) (EC 1.11.1.15) (Cytoplasmic thiol peroxidase 2) (cTPx 2) (Thiol-specific antioxidant protein 2) (Thioredoxin peroxidase type Ib) (TPx type Ib)

 TSA2_YEAST              Reviewed;         196 AA.
Q04120; D6VT78;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 153.
RecName: Full=Peroxiredoxin TSA2 {ECO:0000305};
Short=Prx;
EC=1.11.1.15 {ECO:0000269|PubMed:15210711};
AltName: Full=Cytoplasmic thiol peroxidase 2 {ECO:0000303|PubMed:10681558};
Short=cTPx 2 {ECO:0000303|PubMed:10681558};
AltName: Full=Thiol-specific antioxidant protein 2;
AltName: Full=Thioredoxin peroxidase type Ib {ECO:0000303|PubMed:9888818};
Short=TPx type Ib;
Name=TSA2 {ECO:0000303|PubMed:11741925};
OrderedLocusNames=YDR453C {ECO:0000312|SGD:S000002861};
ORFNames=D9461.38;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=9888818; DOI=10.1021/bi9817818;
Jeong J.S., Kwon S.J., Kang S.W., Rhee S.G., Kim K.;
"Purification and characterization of a second type thioredoxin
peroxidase (type II TPx) from Saccharomyces cerevisiae.";
Biochemistry 38:776-783(1999).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-48.
PubMed=10681558; DOI=10.1074/jbc.275.8.5723;
Park S.G., Cha M.-K., Jeong W., Kim I.-H.;
"Distinct physiological functions of thiol peroxidase isoenzymes in
Saccharomyces cerevisiae.";
J. Biol. Chem. 275:5723-5732(2000).
[5]
FUNCTION.
PubMed=11741925; DOI=10.1074/jbc.M106846200;
Wong C.M., Zhou Y., Ng R.W., Kung Hf H.F., Jin D.Y.;
"Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular
defense against oxidative and nitrosative stress.";
J. Biol. Chem. 277:5385-5394(2002).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
FUNCTION.
PubMed=15163410; DOI=10.1016/j.cell.2004.05.002;
Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H.,
Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y.,
Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.;
"Two enzymes in one; two yeast peroxiredoxins display oxidative
stress-dependent switching from a peroxidase to a molecular chaperone
function.";
Cell 117:625-635(2004).
[8]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
INDUCTION.
PubMed=15210711; DOI=10.1074/jbc.M313773200;
Munhoz D.C., Netto L.E.;
"Cytosolic thioredoxin peroxidase I and II are important defenses of
yeast against organic hydroperoxide insult: catalases and
peroxiredoxins cooperate in the decomposition of H2O2 by yeast.";
J. Biol. Chem. 279:35219-35227(2004).
[9]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT SER-48, AND DISULFIDE
BONDS.
PubMed=26894543; DOI=10.1107/S2059798315023815;
Nielsen M.H., Kidmose R.T., Jenner L.B.;
"Structure of TSA2 reveals novel features of the active-site loop of
peroxiredoxins.";
Acta Crystallogr. D 72:158-167(2016).
-!- 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:10681558,
PubMed:11741925, PubMed:15210711). Can act alternatively as
peroxidase and molecular chaperone. Oxidative stress and heat
shock exposure cause a reversible shift of the protein structure
from low MW species to high MW complexes, triggering a peroxidase-
to-chaperone functional switch. The chaperone function of the
protein enhances resistance to heat shock (PubMed:15163410).
{ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:11741925,
ECO:0000269|PubMed:15163410, ECO:0000269|PubMed:15210711}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:15210711}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=13.8 uM for H(2)O(2) {ECO:0000269|PubMed:15210711};
KM=4.5 uM for cumene hydroperoxide
{ECO:0000269|PubMed:15210711};
KM=5.1 uM for tert-butyl hydroperoxide
{ECO:0000269|PubMed:15210711};
Vmax=0.39 uM/sec/mg enzyme for H(2)O(2)
{ECO:0000269|PubMed:15210711};
Vmax=0.28 uM/sec/mg enzyme for cumene hydroperoxide
{ECO:0000269|PubMed:15210711};
Vmax=0.29 uM/sec/mg enzyme for tert-butyl hydroperoxide
{ECO:0000269|PubMed:15210711};
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10681558}.
-!- INDUCTION: By peroxides. {ECO:0000269|PubMed:15210711}.
-!- 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:P34760}.
-!- MISCELLANEOUS: Present with 4820 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U33007; AAB64886.1; -; Genomic_DNA.
EMBL; BK006938; DAA12288.1; -; Genomic_DNA.
PIR; S69732; S69732.
RefSeq; NP_010741.1; NM_001180761.1.
PDB; 5DVB; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=1-196.
PDB; 5EPT; X-ray; 5.00 A; A/B/C/D/E/F/G/H/I/J=1-196.
PDBsum; 5DVB; -.
PDBsum; 5EPT; -.
ProteinModelPortal; Q04120; -.
SMR; Q04120; -.
BioGrid; 32508; 60.
DIP; DIP-4317N; -.
IntAct; Q04120; 9.
MINT; Q04120; -.
STRING; 4932.YDR453C; -.
MoonProt; Q04120; -.
PeroxiBase; 4467; Sce2CysPrx02.
MaxQB; Q04120; -.
PaxDb; Q04120; -.
PRIDE; Q04120; -.
TopDownProteomics; Q04120; -.
EnsemblFungi; YDR453C; YDR453C; YDR453C.
GeneID; 852064; -.
KEGG; sce:YDR453C; -.
EuPathDB; FungiDB:YDR453C; -.
SGD; S000002861; TSA2.
GeneTree; ENSGT00390000004653; -.
HOGENOM; HOG000022343; -.
InParanoid; Q04120; -.
KO; K03386; -.
OMA; CPANWEE; -.
OrthoDB; EOG092C53IH; -.
BioCyc; YEAST:YDR453C-MONOMER; -.
Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-SCE-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-SCE-6798695; Neutrophil degranulation.
PRO; PR:Q04120; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0051920; F:peroxiredoxin activity; IDA:SGD.
GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:SGD.
GO; GO:0045454; P:cell redox homeostasis; IDA:SGD.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
GO; GO:0006457; P:protein folding; IDA:SGD.
GO; GO:0050821; P:protein stabilization; IDA:CAFA.
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;
Disulfide bond; Isopeptide bond; Oxidoreductase; Peroxidase;
Phosphoprotein; Redox-active center; Reference proteome;
Ubl conjugation.
CHAIN 1 196 Peroxiredoxin TSA2.
/FTId=PRO_0000135096.
DOMAIN 3 161 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 48 48 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000305|PubMed:26894543}.
MOD_RES 174 174 Phosphothreonine.
{ECO:0000250|UniProtKB:P34760}.
DISULFID 48 48 Interchain (with C-171); in linked form.
{ECO:0000244|PDB:5EPT,
ECO:0000269|PubMed:26894543}.
DISULFID 171 171 Interchain (with C-48); in linked form.
{ECO:0000244|PDB:5EPT,
ECO:0000269|PubMed:26894543}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P34760}.
CROSSLNK 89 89 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P34760}.
CROSSLNK 132 132 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P34760}.
MUTAGEN 48 48 C->S: No activity.
{ECO:0000269|PubMed:10681558}.
STRAND 13 18 {ECO:0000244|PDB:5DVB}.
STRAND 21 27 {ECO:0000244|PDB:5DVB}.
HELIX 28 30 {ECO:0000244|PDB:5DVB}.
STRAND 33 39 {ECO:0000244|PDB:5DVB}.
STRAND 45 47 {ECO:0000244|PDB:5DVB}.
HELIX 48 57 {ECO:0000244|PDB:5DVB}.
HELIX 59 64 {ECO:0000244|PDB:5DVB}.
STRAND 67 75 {ECO:0000244|PDB:5DVB}.
HELIX 77 85 {ECO:0000244|PDB:5DVB}.
TURN 88 91 {ECO:0000244|PDB:5DVB}.
STRAND 100 102 {ECO:0000244|PDB:5DVB}.
HELIX 107 111 {ECO:0000244|PDB:5DVB}.
TURN 117 119 {ECO:0000244|PDB:5DVB}.
STRAND 124 129 {ECO:0000244|PDB:5DVB}.
STRAND 133 141 {ECO:0000244|PDB:5DVB}.
HELIX 149 165 {ECO:0000244|PDB:5DVB}.
TURN 184 186 {ECO:0000244|PDB:5DVB}.
HELIX 187 193 {ECO:0000244|PDB:5DVB}.
SEQUENCE 196 AA; 21615 MW; 43CC57C92081D745 CRC64;
MVAEVQKQAP PFKKTAVVDG IFEEISLEKY KGKYVVLAFV PLAFSFVCPT EIVAFSDAAK
KFEDQGAQVL FASTDSEYSL LAWTNLPRKD GGLGPVKVPL LADKNHSLSR DYGVLIEKEG
IALRGLFIID PKGIIRHITI NDLSVGRNVN EALRLVEGFQ WTDKNGTVLP CNWTPGAATI
KPDVKDSKEY FKNANN


Related products :

Catalog number Product name Quantity
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
U1123m CLIA Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,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
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
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
E1123m ELISA 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
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
E1123h ELISA kit 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 pero 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
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
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
E2222m Macrophage 23 kDa stress protein,Mouse,Msp23,Mus musculus,OSF-3,Osteoblast-specific factor 3,Paga,Peroxiredoxin-1,Prdx1,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2
U2222m CLIA kit Macrophage 23 kDa stress protein,Mouse,Msp23,Mus musculus,OSF-3,Osteoblast-specific factor 3,Paga,Peroxiredoxin-1,Prdx1,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductas 96T
U2222m CLIA Macrophage 23 kDa stress protein,Mouse,Msp23,Mus musculus,OSF-3,Osteoblast-specific factor 3,Paga,Peroxiredoxin-1,Prdx1,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
E2222m ELISA Macrophage 23 kDa stress protein,Mouse,Msp23,Mus musculus,OSF-3,Osteoblast-specific factor 3,Paga,Peroxiredoxin-1,Prdx1,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
E2222m ELISA kit Macrophage 23 kDa stress protein,Mouse,Msp23,Mus musculus,OSF-3,Osteoblast-specific factor 3,Paga,Peroxiredoxin-1,Prdx1,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reducta 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