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Peroxiredoxin AHP1 (Prx) (EC 1.11.1.15) (Alkyl hydroperoxide reductase) (AHPC1) (Cytoplasmic thiol peroxidase 3) (cTPx 3) (Thiol-specific antioxidant II) (TSA II) (Thioredoxin peroxidase type II) (TPx type II)

 AHP1_YEAST              Reviewed;         176 AA.
P38013; D6VYA9;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 177.
RecName: Full=Peroxiredoxin AHP1 {ECO:0000305};
Short=Prx;
EC=1.11.1.15 {ECO:0000269|PubMed:10391912, ECO:0000269|PubMed:9888818};
AltName: Full=Alkyl hydroperoxide reductase {ECO:0000303|PubMed:9988687};
Short=AHPC1;
AltName: Full=Cytoplasmic thiol peroxidase 3 {ECO:0000303|PubMed:10681558};
Short=cTPx 3 {ECO:0000303|PubMed:10681558};
AltName: Full=Thiol-specific antioxidant II {ECO:0000303|PubMed:10681558};
Short=TSA II {ECO:0000303|PubMed:10681558};
AltName: Full=Thioredoxin peroxidase type II {ECO:0000303|PubMed:9888818};
Short=TPx type II;
Name=AHP1 {ECO:0000303|PubMed:9988687}; OrderedLocusNames=YLR109W;
ORFNames=L2916, L9354.5;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 90840 / EAY235 / FY23;
PubMed=9090053;
DOI=10.1002/(SICI)1097-0061(19970315)13:3<241::AID-YEA61>3.0.CO;2-#;
Verhasselt P., Volckaert G.;
"Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6,
tRNA-Arg3 and 23 new open reading frames, among which several
homologies to proteins involved in cell division control and to
mammalian growth factors and other animal proteins are found.";
Yeast 13:241-250(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(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 2-8; 16-48; 80-102 AND 114-176, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
Bienvenut W.V., Peters C.;
Submitted (MAY-2005) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 8-15; 33-41; 80-102 AND 125-176, AND URMYLATION.
PubMed=14555475; DOI=10.1128/EC.2.5.930-936.2003;
Goehring A.S., Rivers D.M., Sprague G.F. Jr.;
"Attachment of the ubiquitin-related protein Urm1p to the antioxidant
protein Ahp1p.";
Eukaryot. Cell 2:930-936(2003).
[6]
PROTEIN SEQUENCE OF 16-41; 49-68; 82-96; 114-123 AND 142-150,
POST-TRANSLATIONAL MODIFICATION, DISULFIDE BONDS, 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).
[7]
PARTIAL PROTEIN SEQUENCE OF 33-37; 82-96; 126-139 AND 157-170,
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBUNIT.
PubMed=10391912; DOI=10.1074/jbc.274.28.19714;
Verdoucq L., Vignols F., Jacquot J.-P., Chartier Y., Meyer Y.;
"In vivo characterization of a thioredoxin H target protein defines a
new peroxiredoxin family.";
J. Biol. Chem. 274:19714-19722(1999).
[8]
PROTEIN SEQUENCE OF 82-99.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733; DOI=10.1002/elps.11501501210;
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein
database.";
Electrophoresis 15:1466-1486(1994).
[9]
FUNCTION.
PubMed=10635552; DOI=10.1271/bbb.63.1871;
Farcasanu I.C., Hirata D., Tsuchiya E., Mizuta K., Miyakawa T.;
"Involvement of thioredoxin peroxidase type II (Ahp1p) of
Saccharomyces cerevisiae in Mn2+ homeostasis.";
Biosci. Biotechnol. Biochem. 63:1871-1881(1999).
[10]
FUNCTION, AND SUBUNIT.
PubMed=9988687; DOI=10.1074/jbc.274.8.4537;
Lee J., Spector D., Godon C., Labarre J., Toledano M.B.;
"A new antioxidant with alkyl hydroperoxide defense properties in
yeast.";
J. Biol. Chem. 274:4537-4544(1999).
[11]
FUNCTION, INDUCTION, 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).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-116, 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).
[15]
FUNCTION.
PubMed=20145245; DOI=10.1074/jbc.M109.090142;
Iwai K., Naganuma A., Kuge S.;
"Peroxiredoxin Ahp1 acts as a receptor for alkylhydroperoxides to
induce disulfide bond formation in the Cad1 transcription factor.";
J. Biol. Chem. 285:10597-10604(2010).
[16]
URMYLATION AT LYS-32, AND MUTAGENESIS OF LYS-32.
PubMed=21209336; DOI=10.1073/pnas.1014402108;
Van der Veen A.G., Schorpp K., Schlieker C., Buti L., Damon J.R.,
Spooner E., Ploegh H.L., Jentsch S.;
"Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-
directed protein modifier.";
Proc. Natl. Acad. Sci. U.S.A. 108:1763-1770(2011).
[17]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48 AND LYS-113, 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).
[18]
3D-STRUCTURE MODELING, AND STRUCTURE BY NMR.
PubMed=14640681; DOI=10.1021/bi035551r;
Trivelli X., Krimm I., Ebel C., Verdoucq L., Prouzet-Mauleon V.,
Chartier Y., Tsan P., Lauquin G., Meyer Y., Lancelin J.-M.;
"Characterization of the yeast peroxiredoxin Ahp1 in its reduced
active and overoxidized inactive forms using NMR.";
Biochemistry 42:14139-14149(2003).
[19]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH TRX2, ACTIVE
SITE, DISULFIDE BOND, AND SUBUNIT.
PubMed=22474296; DOI=10.1074/jbc.M112.357368;
Lian F.M., Yu J., Ma X.X., Yu X.J., Chen Y., Zhou C.Z.;
"Structural snapshots of yeast alkyl hydroperoxide reductase Ahp1
peroxiredoxin reveal a novel two-cysteine mechanism of electron
transfer to eliminate reactive oxygen species.";
J. Biol. Chem. 287:17077-17087(2012).
[20]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
Liu M., Wang F., Qiu R., Wu T., Gu S., Tang R., Ji C.;
"Crystal structure of Ahp1 from Saccharomyces cerevisiae in reduced
form.";
Submitted (SEP-2012) to the PDB data bank.
[21]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND DISULFIDE BONDS.
Schultz L., Genu V., Breyer C.A., dos Santos V.F., Guimaraes B.G.,
de Oliveira M.A., Netto L.E.S.;
"Crystal structure of Ahp1 from Saccharomyces cerevisiae.
Investigating the electron transfers.";
Submitted (FEB-2014) to the PDB data bank.
-!- 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. Preferentially
eliminates organic peroxides rather than hydrogen peroxide
(PubMed:10391912, PubMed:9988687, PubMed:10681558). Relays alkyl
hydroperoxides as a signal to the transcription factor CAD1/YAP2
by inducing the formation of intramolecular disulfide bonds in
CAD1, which causes its nuclear accumulation and activation
(PubMed:20145245). Involved in cellular Mn(2+) homeostasis
(PubMed:10635552). {ECO:0000269|PubMed:10391912,
ECO:0000269|PubMed:10635552, ECO:0000269|PubMed:10681558,
ECO:0000269|PubMed:20145245, ECO:0000269|PubMed:9988687}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:10391912, ECO:0000269|PubMed:9888818}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=150 uM for H(2)O(2) {ECO:0000269|PubMed:9888818};
KM=14 uM for H(2)O(2) {ECO:0000269|PubMed:10391912};
KM=8 uM for cumene hydroperoxide {ECO:0000269|PubMed:9888818};
KM=45 uM for tert-butyl hydroperoxide
{ECO:0000269|PubMed:9888818};
KM=76.9 uM for tert-butyl hydroperoxide
{ECO:0000269|PubMed:22474296};
KM=3 uM for TRX1 {ECO:0000269|PubMed:9888818};
KM=2 uM for TRX2 {ECO:0000269|PubMed:9888818};
KM=1.3 uM for TRX2 {ECO:0000269|PubMed:22474296};
Vmax=20 umol/min/mg enzyme for H(2)O(2)
{ECO:0000269|PubMed:9888818};
Vmax=14 umol/min/mg enzyme for cumene hydroperoxide
{ECO:0000269|PubMed:9888818};
Vmax=17 umol/min/mg enzyme for tert-butyl hydroperoxide
{ECO:0000269|PubMed:9888818};
Vmax=17 umol/min/mg enzyme for TRX1
{ECO:0000269|PubMed:9888818};
Vmax=16 umol/min/mg enzyme for TRX2
{ECO:0000269|PubMed:9888818};
pH dependence:
Optimum pH is 6.5. {ECO:0000269|PubMed:9888818};
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
{ECO:0000269|PubMed:10391912, ECO:0000269|PubMed:22474296,
ECO:0000269|PubMed:9888818, ECO:0000269|PubMed:9988687}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10681558}.
-!- INDUCTION: By H(2)O(2). {ECO:0000269|PubMed:10681558}.
-!- PTM: Conjugated to URM1, a ubiquitin-like protein.
{ECO:0000269|PubMed:14555475, ECO:0000269|PubMed:21209336}.
-!- 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 Prx, C(R) is provided by the other
dimeric subunit to form an intersubunit disulfide. The disulfide
is subsequently reduced by thioredoxin.
{ECO:0000305|PubMed:22474296}.
-!- MISCELLANEOUS: Present with 16228 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
{ECO:0000305}.
-!- CAUTION: Biochemical and mutational analysis assigned Cys-120 as
the resolving cysteine (C(R)) (PubMed:9888818). However, crystal
structures showed that Cys-120 is deeply buried within the protein
and revealed formation of a disulfide bond between the peroxidatic
cysteine Cys-62 and the therefore more likely C(R) Cys-31
(PubMed:22474296, Ref.21). {ECO:0000305|PubMed:22474296,
ECO:0000305|PubMed:9888818, ECO:0000305|Ref.21}.
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EMBL; X89514; CAA61687.1; -; Genomic_DNA.
EMBL; Z73281; CAA97676.1; -; Genomic_DNA.
EMBL; U53878; AAB67554.1; -; Genomic_DNA.
EMBL; BK006945; DAA09425.1; -; Genomic_DNA.
PIR; S64946; S64946.
RefSeq; NP_013210.1; NM_001181996.1.
PDB; 4DSQ; X-ray; 2.40 A; A/B/C/D=1-176.
PDB; 4DSR; X-ray; 2.91 A; A/B/C/D=1-176.
PDB; 4DSS; X-ray; 2.10 A; A=1-176.
PDB; 4H86; X-ray; 2.00 A; A=1-176.
PDB; 4OWY; X-ray; 2.20 A; A/B/C/D=1-176.
PDBsum; 4DSQ; -.
PDBsum; 4DSR; -.
PDBsum; 4DSS; -.
PDBsum; 4H86; -.
PDBsum; 4OWY; -.
ProteinModelPortal; P38013; -.
SMR; P38013; -.
BioGrid; 31382; 101.
DIP; DIP-6375N; -.
IntAct; P38013; 13.
MINT; MINT-705985; -.
STRING; 4932.YLR109W; -.
iPTMnet; P38013; -.
COMPLUYEAST-2DPAGE; P38013; -.
MaxQB; P38013; -.
PRIDE; P38013; -.
TopDownProteomics; P38013; -.
EnsemblFungi; YLR109W; YLR109W; YLR109W.
GeneID; 850799; -.
KEGG; sce:YLR109W; -.
EuPathDB; FungiDB:YLR109W; -.
SGD; S000004099; AHP1.
GeneTree; ENSGT00390000018173; -.
HOGENOM; HOG000255884; -.
InParanoid; P38013; -.
KO; K14171; -.
OMA; QRYAMVV; -.
OrthoDB; EOG092C4YDK; -.
BioCyc; YEAST:YLR109W-MONOMER; -.
Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-SCE-5628897; TP53 Regulates Metabolic Genes.
PRO; PR:P38013; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; 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; IGI:SGD.
GO; GO:0010038; P:response to metal ion; IMP:SGD.
InterPro; IPR013740; Redoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF08534; Redoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; 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|Ref.4}.
CHAIN 2 176 Peroxiredoxin AHP1.
/FTId=PRO_0000056610.
DOMAIN 9 176 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 62 62 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000305|PubMed:22474296}.
MOD_RES 2 2 N-acetylserine. {ECO:0000269|Ref.4}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
DISULFID 31 31 Interchain (with C-31 in TRX2);
transient. {ECO:0000269|PubMed:22474296}.
DISULFID 31 31 Interchain (with C-62); in linked form.
{ECO:0000244|PDB:4DSQ,
ECO:0000244|PDB:4OWY,
ECO:0000269|PubMed:22474296}.
DISULFID 62 62 Interchain (with C-31); in linked form.
{ECO:0000244|PDB:4DSQ,
ECO:0000244|PDB:4OWY,
ECO:0000269|PubMed:22474296}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in URM1).
{ECO:0000305|PubMed:21209336}.
CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 113 113 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 31 31 C->S: Abolishes catalytic activity.
{ECO:0000269|PubMed:22474296}.
MUTAGEN 32 32 K->R: Prevents urmylation of AHP1.
{ECO:0000269|PubMed:21209336}.
MUTAGEN 62 62 C->S: Abolishes catalytic activity.
{ECO:0000269|PubMed:22474296}.
MUTAGEN 120 120 C->S: No effect on tert-butyl
hydroperoxide consumption.
{ECO:0000269|PubMed:22474296}.
CONFLICT 21 21 I -> T (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 65 65 S -> V (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 87 87 I -> E (in Ref. 6; AA sequence).
{ECO:0000305}.
TURN 3 6 {ECO:0000244|PDB:4H86}.
STRAND 15 18 {ECO:0000244|PDB:4H86}.
STRAND 23 25 {ECO:0000244|PDB:4H86}.
STRAND 26 28 {ECO:0000244|PDB:4OWY}.
HELIX 29 31 {ECO:0000244|PDB:4H86}.
STRAND 35 38 {ECO:0000244|PDB:4H86}.
HELIX 39 45 {ECO:0000244|PDB:4H86}.
STRAND 47 53 {ECO:0000244|PDB:4H86}.
HELIX 60 64 {ECO:0000244|PDB:4H86}.
HELIX 67 80 {ECO:0000244|PDB:4H86}.
STRAND 85 92 {ECO:0000244|PDB:4H86}.
HELIX 94 103 {ECO:0000244|PDB:4H86}.
STRAND 110 116 {ECO:0000244|PDB:4H86}.
HELIX 118 120 {ECO:0000244|PDB:4H86}.
HELIX 121 125 {ECO:0000244|PDB:4H86}.
STRAND 129 133 {ECO:0000244|PDB:4H86}.
STRAND 136 139 {ECO:0000244|PDB:4H86}.
STRAND 141 147 {ECO:0000244|PDB:4H86}.
STRAND 150 156 {ECO:0000244|PDB:4H86}.
TURN 160 162 {ECO:0000244|PDB:4H86}.
HELIX 169 173 {ECO:0000244|PDB:4H86}.
SEQUENCE 176 AA; 19115 MW; 11B730781306A015 CRC64;
MSDLVNKKFP AGDYKFQYIA ISQSDADSES CKMPQTVEWS KLISENKKVI ITGAPAAFSP
TCTVSHIPGY INYLDELVKE KEVDQVIVVT VDNPFANQAW AKSLGVKDTT HIKFASDPGC
AFTKSIGFEL AVGDGVYWSG RWAMVVENGI VTYAAKETNP GTDVTVSSVE SVLAHL


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