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

Thiol peroxidase (Tpx) (EC 1.11.1.15) (Peroxiredoxin tpx) (Prx) (Scavengase p20) (Thioredoxin peroxidase)

 TPX_ECOLI               Reviewed;         168 AA.
P0A862; P37901; P57669; P76047; P77786;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 119.
RecName: Full=Thiol peroxidase {ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000303|PubMed:7499381};
Short=Tpx {ECO:0000255|HAMAP-Rule:MF_00269};
EC=1.11.1.15 {ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000269|PubMed:12514184};
AltName: Full=Peroxiredoxin tpx {ECO:0000255|HAMAP-Rule:MF_00269};
Short=Prx {ECO:0000255|HAMAP-Rule:MF_00269};
AltName: Full=Scavengase p20 {ECO:0000303|PubMed:9168946};
AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
Name=tpx {ECO:0000255|HAMAP-Rule:MF_00269}; Synonyms=yzzJ;
OrderedLocusNames=b1324, JW1317;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
SUBCELLULAR LOCATION.
STRAIN=K12;
PubMed=7499381; DOI=10.1074/jbc.270.48.28635;
Cha M.-K., Kim H.-K., Kim I.-H.;
"Thioredoxin-linked 'thiol peroxidase' from periplasmic space of
Escherichia coli.";
J. Biol. Chem. 270:28635-28641(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / DH5-alpha;
PubMed=9168946; DOI=10.1006/bbrc.1997.6564;
Zhou Y., Wan X.Y., Wang H.L., Yan Z.Y., Hou Y.D., Jin D.Y.;
"Bacterial scavengase p20 is structurally and functionally related to
peroxiredoxins.";
Biochem. Biophys. Res. Commun. 233:848-852(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 2-19.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J.,
Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A.,
Hochstrasser D.F.;
Submitted (SEP-1994) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 2-16.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[8]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE
SITE, AND MUTAGENESIS OF CYS-61; CYS-82 AND CYS-95.
PubMed=12514184; DOI=10.1074/jbc.M209888200;
Baker L.M., Poole L.B.;
"Catalytic mechanism of thiol peroxidase from Escherichia coli.
Sulfenic acid formation and overoxidation of essential CYS61.";
J. Biol. Chem. 278:9203-9211(2003).
[9]
FUNCTION.
PubMed=14676195; DOI=10.1074/jbc.M312388200;
Cha M.K., Kim W.C., Lim C.J., Kim K., Kim I.H.;
"Escherichia coli periplasmic thiol peroxidase acts as lipid
hydroperoxide peroxidase and the principal antioxidative function
during anaerobic growth.";
J. Biol. Chem. 279:8769-8778(2004).
[10]
SUBCELLULAR LOCATION.
PubMed=19054092; DOI=10.1111/j.1574-6968.2008.01372.x;
Tao K.;
"Subcellular localization and in vivo oxidation-reduction kinetics of
thiol peroxidase in Escherichia coli.";
FEMS Microbiol. Lett. 289:41-45(2008).
[11]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND DISULFIDE BOND.
PubMed=14506251; DOI=10.1074/jbc.M309015200;
Choi J., Choi S., Choi J., Cha M.K., Kim I.H., Shin W.;
"Crystal structure of Escherichia coli thiol peroxidase in the
oxidized state: insights into intramolecular disulfide formation and
substrate binding in atypical 2-Cys peroxiredoxins.";
J. Biol. Chem. 278:49478-49486(2003).
[12]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), DISULFIDE BOND, AND SUBUNIT.
PubMed=19699750; DOI=10.1016/j.jmb.2009.08.040;
Hall A., Sankaran B., Poole L.B., Karplus P.A.;
"Structural changes common to catalysis in the Tpx peroxiredoxin
subfamily.";
J. Mol. Biol. 393:867-881(2009).
[13]
X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 1-168.
PubMed=22691780; DOI=10.1107/S1744309112011487;
Beckham K.S., Byron O., Roe A.J., Gabrielsen M.;
"The structure of an orthorhombic crystal form of a 'forced reduced'
thiol peroxidase reveals lattice formation aided by the presence of
the affinity tag.";
Acta Crystallogr. F 68:522-526(2012).
-!- 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. Has a preference for
alkyl hydroperoxides and acts as lipid peroxidase to inhibit
bacterial membrane oxidation. Acts as principal antioxidant during
anaerobic growth. {ECO:0000255|HAMAP-Rule:MF_00269,
ECO:0000269|PubMed:12514184, ECO:0000269|PubMed:14676195}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000269|PubMed:12514184}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1730 uM for H(2)O(2) {ECO:0000269|PubMed:12514184};
KM=9.1 uM for cumene hydroperoxide
{ECO:0000269|PubMed:12514184};
KM=25.5 uM for Trx1 (using H(2)O(2) as substrate)
{ECO:0000269|PubMed:12514184};
KM=22.5 uM for Trx1 (using cumene hydroperoxide as substrate)
{ECO:0000269|PubMed:12514184};
Note=kcat is 76.0 sec(-1) with H(2)O(2) as substrate and 70.1
sec(-1) with cumene hydroperoxide as substrate.
{ECO:0000269|PubMed:12514184};
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00269,
ECO:0000269|PubMed:19699750}.
-!- INTERACTION:
P0A8E1:ycfP; NbExp=3; IntAct=EBI-369411, EBI-9129402;
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:7499381}.
Cytoplasm {ECO:0000269|PubMed:19054092}. Note=Forms a mixed
disulfide with cytoplasmic thioredoxin (trx1).
{ECO:0000269|PubMed:19054092}.
-!- 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 atypical 2-Cys peroxiredoxin, C(R) is present in
the same subunit to form an intramolecular disulfide. The
disulfide is subsequently reduced by thioredoxin.
{ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000305|PubMed:12514184}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
{ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U33213; AAC43517.1; -; Genomic_DNA.
EMBL; U93212; AAC45284.1; -; Genomic_DNA.
EMBL; U00096; AAC74406.1; -; Genomic_DNA.
EMBL; AP009048; BAA14906.1; -; Genomic_DNA.
PIR; JC5504; JC5504.
RefSeq; NP_415840.1; NC_000913.3.
RefSeq; WP_000084387.1; NZ_LN832404.1.
PDB; 1QXH; X-ray; 2.20 A; A/B=2-168.
PDB; 3HVS; X-ray; 1.80 A; A/B=2-168.
PDB; 3HVV; X-ray; 1.75 A; A=2-168.
PDB; 3HVX; X-ray; 2.12 A; A/B/C/D=2-168.
PDB; 3I43; X-ray; 2.80 A; A/B=2-168.
PDB; 4AF2; X-ray; 1.97 A; A=1-168.
PDBsum; 1QXH; -.
PDBsum; 3HVS; -.
PDBsum; 3HVV; -.
PDBsum; 3HVX; -.
PDBsum; 3I43; -.
PDBsum; 4AF2; -.
ProteinModelPortal; P0A862; -.
SMR; P0A862; -.
BioGrid; 4260151; 139.
BioGrid; 850247; 1.
DIP; DIP-31857N; -.
IntAct; P0A862; 9.
STRING; 316385.ECDH10B_1443; -.
PeroxiBase; 6007; EcoTPx.
SWISS-2DPAGE; P0A862; -.
EPD; P0A862; -.
PaxDb; P0A862; -.
PRIDE; P0A862; -.
EnsemblBacteria; AAC74406; AAC74406; b1324.
EnsemblBacteria; BAA14906; BAA14906; BAA14906.
GeneID; 945880; -.
KEGG; ecj:JW1317; -.
KEGG; eco:b1324; -.
PATRIC; fig|1411691.4.peg.954; -.
EchoBASE; EB2538; -.
EcoGene; EG12672; tpx.
eggNOG; ENOG4108V1J; Bacteria.
eggNOG; COG2077; LUCA.
HOGENOM; HOG000022345; -.
InParanoid; P0A862; -.
KO; K11065; -.
OMA; ITQEPNY; -.
PhylomeDB; P0A862; -.
BioCyc; EcoCyc:G6660-MONOMER; -.
BioCyc; MetaCyc:G6660-MONOMER; -.
BRENDA; 1.11.1.7; 2026.
EvolutionaryTrace; P0A862; -.
PRO; PR:P0A862; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0032843; F:hydroperoxide reductase activity; IDA:EcoCyc.
GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:EcoCyc.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:EcoCyc.
CDD; cd03014; PRX_Atyp2cys; 1.
HAMAP; MF_00269; Tpx; 1.
InterPro; IPR013740; Redoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
InterPro; IPR002065; TPX.
InterPro; IPR018219; Tpx_CS.
Pfam; PF08534; Redoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
PROSITE; PS01265; TPX; 1.
1: Evidence at protein level;
3D-structure; Antioxidant; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Oxidoreductase; Periplasm;
Peroxidase; Redox-active center; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9298646,
ECO:0000269|Ref.6}.
CHAIN 2 168 Thiol peroxidase.
/FTId=PRO_0000187877.
DOMAIN 19 168 Thioredoxin. {ECO:0000255|HAMAP-
Rule:MF_00269}.
ACT_SITE 61 61 Cysteine sulfenic acid (-SOH)
intermediate. {ECO:0000255|HAMAP-
Rule:MF_00269,
ECO:0000269|PubMed:12514184}.
DISULFID 61 95 Redox-active. {ECO:0000244|PDB:1QXH,
ECO:0000244|PDB:3HVS,
ECO:0000244|PDB:3I43, ECO:0000255|HAMAP-
Rule:MF_00269,
ECO:0000269|PubMed:14506251,
ECO:0000269|PubMed:19699750}.
MUTAGEN 61 61 C->S: Abolishes catalytic activity.
{ECO:0000269|PubMed:12514184}.
MUTAGEN 82 82 C->S: Reduces catalytic activity by 28%.
{ECO:0000269|PubMed:12514184}.
MUTAGEN 95 95 C->S: Reduces catalytic activity by 80%.
{ECO:0000269|PubMed:12514184}.
CONFLICT 61 61 C -> Y (in Ref. 1; AAC43517).
{ECO:0000305}.
STRAND 3 7 {ECO:0000244|PDB:3HVV}.
STRAND 10 14 {ECO:0000244|PDB:3HVV}.
STRAND 29 31 {ECO:0000244|PDB:3HVV}.
STRAND 37 39 {ECO:0000244|PDB:3HVV}.
HELIX 40 43 {ECO:0000244|PDB:3HVV}.
STRAND 46 52 {ECO:0000244|PDB:3HVV}.
STRAND 56 59 {ECO:0000244|PDB:3HVX}.
HELIX 61 71 {ECO:0000244|PDB:3HVV}.
HELIX 72 74 {ECO:0000244|PDB:3HVV}.
STRAND 75 86 {ECO:0000244|PDB:3HVV}.
HELIX 88 98 {ECO:0000244|PDB:3HVV}.
STRAND 102 107 {ECO:0000244|PDB:3HVV}.
HELIX 112 117 {ECO:0000244|PDB:3HVV}.
TURN 126 129 {ECO:0000244|PDB:3HVV}.
STRAND 133 138 {ECO:0000244|PDB:3HVV}.
STRAND 142 149 {ECO:0000244|PDB:3HVV}.
HELIX 159 164 {ECO:0000244|PDB:3HVV}.
SEQUENCE 168 AA; 17835 MW; F95F39094A07DBB2 CRC64;
MSQTVHFQGN PVTVANSIPQ AGSKAQTFTL VAKDLSDVTL GQFAGKRKVL NIFPSIDTGV
CAASVRKFNQ LATEIDNTVV LCISADLPFA QSRFCGAEGL NNVITLSTFR NAEFLQAYGV
AIADGPLKGL AARAVVVIDE NDNVIFSQLV DEITTEPDYE AALAVLKA


Related products :

Catalog number Product name Quantity
U1123p CLIA 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
E1123p ELISA kit 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
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 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 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
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
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
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
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
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
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


 

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