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Peroxiredoxin TSA1 (Prx) (EC 1.11.1.15) (Cytoplasmic thiol peroxidase 1) (cTPx 1) (Protector protein) (PRP) (Thiol-specific antioxidant protein 1) (Thioredoxin peroxidase type Ia) (TPx type Ia) (Thioredoxin-dependent peroxide reductase)

 TSA1_YEAST              Reviewed;         196 AA.
P34760; D6VZE6;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 164.
RecName: Full=Peroxiredoxin TSA1 {ECO:0000305};
Short=Prx;
EC=1.11.1.15 {ECO:0000269|PubMed:9888818};
AltName: Full=Cytoplasmic thiol peroxidase 1 {ECO:0000303|PubMed:10681558};
Short=cTPx 1 {ECO:0000303|PubMed:10681558};
AltName: Full=Protector protein {ECO:0000303|PubMed:2895105};
Short=PRP;
AltName: Full=Thiol-specific antioxidant protein 1 {ECO:0000303|PubMed:8344960};
AltName: Full=Thioredoxin peroxidase type Ia {ECO:0000303|PubMed:9888818};
Short=TPx type Ia;
AltName: Full=Thioredoxin-dependent peroxide reductase {ECO:0000303|PubMed:7961686};
Name=TSA1 {ECO:0000303|PubMed:8344960}; Synonyms=TPX1, TSA, ZRG14;
OrderedLocusNames=YML028W {ECO:0000312|SGD:S000004490};
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE OF 2-13; 62-66; 79-87;
90-94; 137-143; 148-153; 155-161 AND 192-196, CLEAVAGE OF INITIATOR
METHIONINE, AND SUBCELLULAR LOCATION.
STRAIN=JD7-7C;
PubMed=8344960;
Chae H.Z., Kim I.-H., Kim K., Rhee S.G.;
"Cloning, sequencing, and mutation of thiol-specific antioxidant gene
of Saccharomyces cerevisiae.";
J. Biol. Chem. 268:16815-16821(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[3]
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).
[4]
PROTEIN SEQUENCE OF 15-19; 32-38; 155-159 AND 165-169, SUBUNIT, ACTIVE
SITE, DISULFIDE BOND, AND MUTAGENESIS OF CYS-48 AND CYS-171.
PubMed=8041739;
Chae H.Z., Uhm T.B., Rhee S.G.;
"Dimerization of thiol-specific antioxidant and the essential role of
cysteine 47.";
Proc. Natl. Acad. Sci. U.S.A. 91:7022-7026(1994).
[5]
FUNCTION.
PubMed=2895105;
Kim K., Kim I.H., Lee K.Y., Rhee S.G., Stadtman E.R.;
"The isolation and purification of a specific 'protector' protein
which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-
function oxidation system.";
J. Biol. Chem. 263:4704-4711(1988).
[6]
FUNCTION, AND MUTAGENESIS OF CYS-48 AND CYS-171.
PubMed=7961686;
Chae H.Z., Chung S.J., Rhee S.G.;
"Thioredoxin-dependent peroxide reductase from yeast.";
J. Biol. Chem. 269:27670-27678(1994).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[9]
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).
[10]
DISULFIDE BOND WITH SRX1.
PubMed=14586471; DOI=10.1038/nature02075;
Biteau B., Labarre J., Toledano M.B.;
"ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae
sulphiredoxin.";
Nature 425:980-984(2003).
[11]
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).
[12]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
[13]
FUNCTION.
PubMed=15706081; DOI=10.1089/ars.2005.7.327;
Okazaki S., Naganuma A., Kuge S.;
"Peroxiredoxin-mediated redox regulation of the nuclear localization
of Yap1, a transcription factor in budding yeast.";
Antioxid. Redox Signal. 7:327-334(2005).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18271751; DOI=10.1042/BJ20071634;
Trotter E.W., Rand J.D., Vickerstaff J., Grant C.M.;
"The yeast Tsa1 peroxiredoxin is a ribosome-associated antioxidant.";
Biochem. J. 412:73-80(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[16]
FUNCTION, AND INTERACTION WITH YAP1.
PubMed=19106090; DOI=10.1074/jbc.M807583200;
Tachibana T., Okazaki S., Murayama A., Naganuma A., Nomoto A.,
Kuge S.;
"A major peroxiredoxin-induced activation of Yap1 transcription factor
is mediated by reduction-sensitive disulfide bonds and reveals a low
level of transcriptional activation.";
J. Biol. Chem. 284:4464-4472(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[18]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-89 AND LYS-132,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24424024; DOI=10.1242/jcs.144022;
Weids A.J., Grant C.M.;
"The yeast peroxiredoxin Tsa1 protects against protein-aggregate-
induced oxidative stress.";
J. Cell Sci. 127:1327-1335(2014).
[20]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF MUTANT SER-48 IN COMPLEX
WITH DITHIOTHREITOL.
PubMed=22985967; DOI=10.1016/j.jmb.2012.09.008;
Tairum C.A. Jr., de Oliveira M.A., Horta B.B., Zara F.J., Netto L.E.;
"Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50
and Arg146 for the reduction of yeast Tsa1 by thioredoxin.";
J. Mol. Biol. 424:28-41(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 and as sensor of
hydrogen peroxide-mediated signaling events (PubMed:2895105,
PubMed:7961686, PubMed:10681558, PubMed:15210711,
PubMed:19106090). Protects the cell against the oxidative stress
caused by nascent-protein misfolding and aggregation
(PubMed:24424024). Relays hydrogen peroxide as a signal to the
transcription factor YAP1 by inducing the formation of
intramolecular disulfide bonds in YAP1, which causes its nuclear
accumulation and activation (PubMed:15706081, PubMed:19106090).
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:15163410, ECO:0000269|PubMed:15210711,
ECO:0000269|PubMed:15706081, ECO:0000269|PubMed:19106090,
ECO:0000269|PubMed:24424024, ECO:0000269|PubMed:2895105,
ECO:0000269|PubMed:7961686}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:9888818}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3 uM for H(2)O(2) {ECO:0000269|PubMed:9888818};
KM=4 uM for cumene hydroperoxide {ECO:0000269|PubMed:9888818};
KM=10 uM for tert-butyl hydroperoxide
{ECO:0000269|PubMed:9888818};
KM=2 uM for TRX1 {ECO:0000269|PubMed:9888818};
KM=3 uM for TRX2 {ECO:0000269|PubMed:9888818};
KM=12 uM for H(2)O(2) {ECO:0000269|PubMed:15210711};
KM=17.1 uM for cumene hydroperoxide
{ECO:0000269|PubMed:15210711};
KM=7.9 uM for tert-butyl hydroperoxide
{ECO:0000269|PubMed:15210711};
Vmax=4.8 umol/min/mg enzyme for H(2)O(2)
{ECO:0000269|PubMed:9888818};
Vmax=2.2 umol/min/mg enzyme for cumene hydroperoxide
{ECO:0000269|PubMed:9888818};
Vmax=2.4 umol/min/mg enzyme for tert-butyl hydroperoxide
{ECO:0000269|PubMed:9888818};
Vmax=5.5 umol/min/mg enzyme for TRX1
{ECO:0000269|PubMed:9888818};
Vmax=5.5 umol/min/mg enzyme for TRX2
{ECO:0000269|PubMed:9888818};
Vmax=0.66 uM/sec/mg enzyme for H(2)O(2)
{ECO:0000269|PubMed:15210711};
Vmax=0.56 uM/sec/mg enzyme for cumene hydroperoxide
{ECO:0000269|PubMed:15210711};
Vmax=0.61 uM/sec/mg enzyme for tert-butyl hydroperoxide
{ECO:0000269|PubMed:15210711};
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation
(PubMed:8041739). Interacts with YAP1 via transient disulfide
linkages (PubMed:19106090). {ECO:0000269|PubMed:19106090,
ECO:0000269|PubMed:8041739}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10681558,
ECO:0000269|PubMed:18271751, ECO:0000269|PubMed:24424024,
ECO:0000269|PubMed:8344960}. Note=Associates with ribosomes
(PubMed:18271751). Colocalizes with sites of protein aggregation
adjacent to active mitochondria (PubMed:24424024).
{ECO:0000269|PubMed:18271751, ECO:0000269|PubMed:24424024}.
-!- PTM: The enzyme can be inactivated by further oxidation of the
cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H)
instead of its condensation to a disulfide bond. It can be
reactivated by forming a transient disulfide bond with
sulfiredoxin SRX1, which reduces the cysteine sulfinic acid in an
ATP- and Mg-dependent manner. {ECO:0000269|PubMed:14586471}.
-!- 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:0000305|PubMed:8041739}.
-!- MISCELLANEOUS: Present with 378000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L14640; AAA16374.1; -; Unassigned_DNA.
EMBL; Z46659; CAA86627.1; -; Genomic_DNA.
EMBL; BK006946; DAA09870.1; -; Genomic_DNA.
PIR; A47362; A47362.
RefSeq; NP_013684.1; NM_001182386.1.
PDB; 3SBC; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J=1-196.
PDBsum; 3SBC; -.
ProteinModelPortal; P34760; -.
SMR; P34760; -.
BioGrid; 35141; 559.
DIP; DIP-1667N; -.
IntAct; P34760; 38.
MINT; MINT-408012; -.
STRING; 4932.YML028W; -.
MoonProt; P34760; -.
PeroxiBase; 4465; Sce2CysPrx01.
iPTMnet; P34760; -.
SWISS-2DPAGE; P34760; -.
MaxQB; P34760; -.
PRIDE; P34760; -.
TopDownProteomics; P34760; -.
EnsemblFungi; YML028W; YML028W; YML028W.
GeneID; 854980; -.
KEGG; sce:YML028W; -.
EuPathDB; FungiDB:YML028W; -.
SGD; S000004490; TSA1.
GeneTree; ENSGT00390000004653; -.
HOGENOM; HOG000022343; -.
InParanoid; P34760; -.
KO; K03386; -.
OMA; TAVHNGE; -.
OrthoDB; EOG092C53IH; -.
BioCyc; YEAST:YML028W-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:P34760; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005622; C:intracellular; IDA:CAFA.
GO; GO:0005844; C:polysome; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IMP:CAFA.
GO; GO:0019207; F:kinase regulator activity; IMP:SGD.
GO; GO:0051920; F:peroxiredoxin activity; IDA:SGD.
GO; GO:0043022; F:ribosome binding; IDA:SGD.
GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:SGD.
GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
GO; GO:0045454; P:cell redox homeostasis; IDA:SGD.
GO; GO:0034605; P:cellular response to heat; IMP:CAFA.
GO; GO:0071447; P:cellular response to hydroperoxide; IMP:CAFA.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:SGD.
GO; GO:0061077; P:chaperone-mediated protein folding; IMP:CAFA.
GO; GO:0000077; P:DNA damage checkpoint; IGI:SGD.
GO; GO:0042262; P:DNA protection; IMP:SGD.
GO; GO:0090344; P:negative regulation of cell aging; IMP:SGD.
GO; GO:0060548; P:negative regulation of cell death; IMP:CAFA.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IMP:CAFA.
GO; GO:0006457; P:protein folding; IDA:SGD.
GO; GO:0051258; P:protein polymerization; IMP:CAFA.
GO; GO:0050821; P:protein stabilization; IMP:CAFA.
GO; GO:0006111; P:regulation of gluconeogenesis; IMP:SGD.
GO; GO:0001302; P:replicative cell aging; IMP:SGD.
GO; GO:0033194; P:response to hydroperoxide; IMP:SGD.
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; Isopeptide bond;
Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8344960}.
CHAIN 2 196 Peroxiredoxin TSA1.
/FTId=PRO_0000135095.
DOMAIN 3 161 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
REGION 45 47 Substrate binding. {ECO:0000244|PDB:3SBC,
ECO:0000269|PubMed:22985967}.
ACT_SITE 48 48 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000305|PubMed:8041739}.
BINDING 124 124 Substrate. {ECO:0000244|PDB:3SBC,
ECO:0000269|PubMed:22985967}.
SITE 45 45 Important for catalytic activity, helps
activating the peroxidatic cysteine
through H-bonding.
MOD_RES 174 174 Phosphothreonine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
DISULFID 48 48 Interchain (with C-171); in linked form.
{ECO:0000305|PubMed:7961686}.
DISULFID 48 48 Interchain (with C-84 in SRX1);
transient. {ECO:0000269|PubMed:14586471}.
DISULFID 171 171 Interchain (with C-48); in linked form.
{ECO:0000305|PubMed:7961686}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 89 89 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 132 132 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 48 48 C->S: Exists mainly as monomer. Has no
peroxiredoxin activity. Fails to protect
glutamine synthetase against damage by
DTT oxidation.
{ECO:0000269|PubMed:7961686,
ECO:0000269|PubMed:8041739}.
MUTAGEN 171 171 C->S: Exists mainly as monomer. Has no
peroxiredoxin activity.
{ECO:0000269|PubMed:7961686,
ECO:0000269|PubMed:8041739}.
STRAND 14 18 {ECO:0000244|PDB:3SBC}.
STRAND 21 25 {ECO:0000244|PDB:3SBC}.
HELIX 27 30 {ECO:0000244|PDB:3SBC}.
STRAND 33 39 {ECO:0000244|PDB:3SBC}.
HELIX 47 64 {ECO:0000244|PDB:3SBC}.
STRAND 67 75 {ECO:0000244|PDB:3SBC}.
HELIX 77 84 {ECO:0000244|PDB:3SBC}.
HELIX 88 90 {ECO:0000244|PDB:3SBC}.
STRAND 100 102 {ECO:0000244|PDB:3SBC}.
HELIX 107 112 {ECO:0000244|PDB:3SBC}.
TURN 117 119 {ECO:0000244|PDB:3SBC}.
STRAND 124 129 {ECO:0000244|PDB:3SBC}.
STRAND 133 141 {ECO:0000244|PDB:3SBC}.
HELIX 149 165 {ECO:0000244|PDB:3SBC}.
TURN 184 186 {ECO:0000244|PDB:3SBC}.
HELIX 187 194 {ECO:0000244|PDB:3SBC}.
SEQUENCE 196 AA; 21590 MW; 9ACF40E410F2C04A CRC64;
MVAQVQKQAP TFKKTAVVDG VFDEVSLDKY KGKYVVLAFI PLAFTFVCPT EIIAFSEAAK
KFEEQGAQVL FASTDSEYSL LAWTNIPRKE GGLGPINIPL LADTNHSLSR DYGVLIEEEG
VALRGLFIID PKGVIRHITI NDLPVGRNVD EALRLVEAFQ WTDKNGTVLP CNWTPGAATI
KPTVEDSKEY FEAANK


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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
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
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
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
E2222r HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2
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
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


 

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