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Thioredoxin, mitochondrial (MTRX) (Mt-Trx) (Thioredoxin-2)

 THIOM_HUMAN             Reviewed;         166 AA.
Q99757; Q5JZA0; Q6FH60; Q9UH29;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
02-MAY-2002, sequence version 2.
30-AUG-2017, entry version 172.
RecName: Full=Thioredoxin, mitochondrial;
Short=MTRX;
Short=Mt-Trx;
AltName: Full=Thioredoxin-2;
Flags: Precursor;
Name=TXN2; Synonyms=TRX2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Osteosarcoma;
PubMed=12032145; DOI=10.1074/jbc.M202026200;
Chen Y., Cai J., Murphy T.J., Jones D.P.;
"Overexpressed human mitochondrial thioredoxin confers resistance to
oxidant-induced apoptosis in human osteosarcoma cells.";
J. Biol. Chem. 277:33242-33248(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Liver;
PubMed=12080052; DOI=10.1074/jbc.M203036200;
Damdimopoulos A.E., Miranda-Vizuete A., Pelto-Huikko M.,
Gustafsson J.-A., Spyrou G.;
"Human mitochondrial thioredoxin. Involvement in mitochondrial
membrane potential and cell death.";
J. Biol. Chem. 277:33249-33257(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lens;
Reddy P.G., Bhuyan D.K., Bhuyan K.C.;
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas, and Placenta;
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).
[9]
PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 60-74.
TISSUE=Leukemic T-cell;
PubMed=19892738; DOI=10.1073/pnas.0908958106;
Xu G., Shin S.B., Jaffrey S.R.;
"Global profiling of protease cleavage sites by chemoselective
labeling of protein N-termini.";
Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER LEU-59, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
INVOLVEMENT IN COXPD29, AND FUNCTION.
PubMed=26626369; DOI=10.1093/brain/awv350;
Holzerova E., Danhauser K., Haack T.B., Kremer L.S., Melcher M.,
Ingold I., Kobayashi S., Terrile C., Wolf P., Schaper J.,
Mayatepek E., Baertling F., Friedmann Angeli J.P., Conrad M.,
Strom T.M., Meitinger T., Prokisch H., Distelmaier F.;
"Human thioredoxin 2 deficiency impairs mitochondrial redox
homeostasis and causes early-onset neurodegeneration.";
Brain 139:346-354(2016).
[14]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 60-166, AND SUBUNIT.
PubMed=16195549; DOI=10.1110/ps.051632905;
Smeets A., Evrard C., Landtmeters M., Marchand C., Knoops B.,
Declercq J.-P.;
"Crystal structures of oxidized and reduced forms of human
mitochondrial thioredoxin 2.";
Protein Sci. 14:2610-2621(2005).
-!- FUNCTION: Important for the control of mitochondrial reactive
oxygen species homeostasis, apoptosis regulation and cell
viability. Possesses a dithiol-reducing activity.
{ECO:0000269|PubMed:12032145, ECO:0000269|PubMed:12080052,
ECO:0000269|PubMed:26626369}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16195549}.
-!- INTERACTION:
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-2932492, EBI-741181;
P63010:AP2B1; NbExp=3; IntAct=EBI-2932492, EBI-432924;
Q96M63:CCDC114; NbExp=3; IntAct=EBI-2932492, EBI-10173858;
P32321:DCTD; NbExp=3; IntAct=EBI-2932492, EBI-739870;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-2932492, EBI-10175124;
Q96D09:GPRASP2; NbExp=3; IntAct=EBI-2932492, EBI-473189;
Q6A162:KRT40; NbExp=3; IntAct=EBI-2932492, EBI-10171697;
P43364-2:MAGEA11; NbExp=3; IntAct=EBI-2932492, EBI-10178634;
Q15555:MAPRE2; NbExp=5; IntAct=EBI-2932492, EBI-739717;
Q9UPY8:MAPRE3; NbExp=7; IntAct=EBI-2932492, EBI-726739;
Q96HT8:MRFAP1L1; NbExp=5; IntAct=EBI-2932492, EBI-748896;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-2932492, EBI-742948;
Q96CD2:PPCDC; NbExp=5; IntAct=EBI-2932492, EBI-724333;
P61289:PSME3; NbExp=3; IntAct=EBI-2932492, EBI-355546;
Q9UJ41:RABGEF1; NbExp=3; IntAct=EBI-2932492, EBI-913954;
Q8IUH3:RBM45; NbExp=3; IntAct=EBI-2932492, EBI-2512147;
Q96HR9:REEP6; NbExp=3; IntAct=EBI-2932492, EBI-750345;
P49247:RPIA; NbExp=5; IntAct=EBI-2932492, EBI-744831;
Q8IZE3:SCYL3; NbExp=3; IntAct=EBI-2932492, EBI-1380680;
P02549:SPTA1; NbExp=4; IntAct=EBI-2932492, EBI-375617;
O43805:SSNA1; NbExp=5; IntAct=EBI-2932492, EBI-2515299;
Q9UNE7:STUB1; NbExp=3; IntAct=EBI-2932492, EBI-357085;
Q96CG3:TIFA; NbExp=3; IntAct=EBI-2932492, EBI-740711;
P19474:TRIM21; NbExp=5; IntAct=EBI-2932492, EBI-81290;
Q15654:TRIP6; NbExp=3; IntAct=EBI-2932492, EBI-742327;
Q8N1B4:VPS52; NbExp=5; IntAct=EBI-2932492, EBI-2799833;
O43829:ZBTB14; NbExp=3; IntAct=EBI-2932492, EBI-10176632;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12032145,
ECO:0000269|PubMed:12080052}.
-!- TISSUE SPECIFICITY: Widely expressed in adult (at protein level)
and fetal tissues. {ECO:0000269|PubMed:12032145,
ECO:0000269|PubMed:12080052}.
-!- DISEASE: Combined oxidative phosphorylation deficiency 29
(COXPD29) [MIM:616811]: An autosomal recessive, infantile-onset,
neurodegenerative disorder characterized by decreased activities
of mitochondrial respiratory complexes I and III, severe
cerebellar atrophy, epilepsy, dystonia, optic atrophy, and
peripheral neuropathy. {ECO:0000269|PubMed:26626369}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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EMBL; AF480262; AAN05576.1; -; mRNA.
EMBL; U78678; AAB41631.1; -; mRNA.
EMBL; AF276920; AAF86467.1; -; mRNA.
EMBL; CR456601; CAG30487.1; -; mRNA.
EMBL; CR541896; CAG46694.1; -; mRNA.
EMBL; CR541917; CAG46715.1; -; mRNA.
EMBL; AL022313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60103.1; -; Genomic_DNA.
EMBL; BC013726; AAH13726.1; -; mRNA.
EMBL; BC050610; AAH50610.1; -; mRNA.
CCDS; CCDS13928.1; -.
RefSeq; NP_036605.2; NM_012473.3.
RefSeq; XP_006724289.1; XM_006724226.1.
UniGene; Hs.211929; -.
PDB; 1UVZ; X-ray; 2.01 A; A/B/C/D/E/F=60-166.
PDB; 1W4V; X-ray; 1.80 A; A/B/C/D/E/F=60-166.
PDB; 1W89; X-ray; 2.00 A; A/B/C/D/E/F=60-166.
PDBsum; 1UVZ; -.
PDBsum; 1W4V; -.
PDBsum; 1W89; -.
ProteinModelPortal; Q99757; -.
SMR; Q99757; -.
BioGrid; 117356; 59.
IntAct; Q99757; 67.
STRING; 9606.ENSP00000216185; -.
BindingDB; Q99757; -.
ChEMBL; CHEMBL2189153; -.
iPTMnet; Q99757; -.
PhosphoSitePlus; Q99757; -.
BioMuta; TXN2; -.
DMDM; 20455529; -.
EPD; Q99757; -.
MaxQB; Q99757; -.
PaxDb; Q99757; -.
PeptideAtlas; Q99757; -.
PRIDE; Q99757; -.
TopDownProteomics; Q99757; -.
DNASU; 25828; -.
Ensembl; ENST00000216185; ENSP00000216185; ENSG00000100348.
Ensembl; ENST00000403313; ENSP00000385393; ENSG00000100348.
GeneID; 25828; -.
KEGG; hsa:25828; -.
UCSC; uc003apk.2; human.
CTD; 25828; -.
DisGeNET; 25828; -.
GeneCards; TXN2; -.
HGNC; HGNC:17772; TXN2.
HPA; CAB008681; -.
HPA; HPA000994; -.
MIM; 609063; gene.
MIM; 616811; phenotype.
neXtProt; NX_Q99757; -.
OpenTargets; ENSG00000100348; -.
PharmGKB; PA38245; -.
eggNOG; KOG0910; Eukaryota.
eggNOG; COG0526; LUCA.
GeneTree; ENSGT00530000064086; -.
HOVERGEN; HBG009243; -.
InParanoid; Q99757; -.
KO; K03671; -.
OMA; CRMLTPR; -.
OrthoDB; EOG091G0UDG; -.
PhylomeDB; Q99757; -.
TreeFam; TF314517; -.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
ChiTaRS; TXN2; human.
EvolutionaryTrace; Q99757; -.
GeneWiki; TXN2; -.
GenomeRNAi; 25828; -.
PRO; PR:Q99757; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100348; -.
CleanEx; HS_TXN2; -.
ExpressionAtlas; Q99757; baseline and differential.
Genevisible; Q99757; HS.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:CACAO.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:Ensembl.
GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
InterPro; IPR005746; Thioredoxin.
InterPro; IPR012336; Thioredoxin-like_fold.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR01068; thioredoxin; 1.
PROSITE; PS00194; THIOREDOXIN_1; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Disulfide bond; Electron transport;
Mitochondrion; Neurodegeneration; Primary mitochondrial disease;
Redox-active center; Reference proteome; Transit peptide; Transport.
TRANSIT 1 59 Mitochondrion.
{ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:19892738}.
CHAIN 60 166 Thioredoxin, mitochondrial.
/FTId=PRO_0000034150.
DOMAIN 61 166 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 90 90 Nucleophile. {ECO:0000250}.
ACT_SITE 93 93 Nucleophile. {ECO:0000250}.
SITE 84 84 Deprotonates C-terminal active site Cys.
{ECO:0000250}.
SITE 91 91 Contributes to redox potential value.
{ECO:0000250}.
SITE 92 92 Contributes to redox potential value.
{ECO:0000250}.
MOD_RES 152 152 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 152 152 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P97493}.
DISULFID 90 93 Redox-active.
CONFLICT 30 30 R -> K (in Ref. 2; AAB41631 and 3;
AAF86467). {ECO:0000305}.
STRAND 60 63 {ECO:0000244|PDB:1W4V}.
HELIX 67 73 {ECO:0000244|PDB:1W4V}.
TURN 74 76 {ECO:0000244|PDB:1W4V}.
STRAND 81 86 {ECO:0000244|PDB:1W4V}.
HELIX 91 106 {ECO:0000244|PDB:1W4V}.
TURN 107 109 {ECO:0000244|PDB:1W4V}.
STRAND 110 117 {ECO:0000244|PDB:1W4V}.
TURN 118 121 {ECO:0000244|PDB:1W4V}.
HELIX 122 127 {ECO:0000244|PDB:1W4V}.
STRAND 132 140 {ECO:0000244|PDB:1W4V}.
STRAND 143 150 {ECO:0000244|PDB:1W4V}.
HELIX 154 165 {ECO:0000244|PDB:1W4V}.
SEQUENCE 166 AA; 18383 MW; C4CA8CDAD485D499 CRC64;
MAQRLLLRRF LASVISRKPS QGQWPPLTSR ALQTPQCSPG GLTVTPNPAR TIYTTRISLT
TFNIQDGPDF QDRVVNSETP VVVDFHAQWC GPCKILGPRL EKMVAKQHGK VVMAKVDIDD
HTDLAIEYEV SAVPTVLAMK NGDVVDKFVG IKDEDQLEAF LKKLIG


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EIAAB44637 Endoplasmic reticulum resident protein 46,ER protein 46,ERp46,Mouse,Mus musculus,PC-TRP,Plasma cell-specific thioredoxin-related protein,Thioredoxin domain-containing protein 5,Thioredoxin-like protei
EIAAB44153 Homo sapiens,Human,TGR,Thioredoxin and glutathione reductase,Thioredoxin reductase 3,Thioredoxin reductase TR2,TRXR3,TXNRD3
EIAAB44613 14 kDa thioredoxin-related protein,Homo sapiens,Human,Protein 42-9-9,Thioredoxin domain-containing protein 17,Thioredoxin-like protein 5,TRP14,TXNDC17,TXNL5
EIAAB44154 Mouse,Mus musculus,Tgr,Thioredoxin and glutathione reductase,Thioredoxin reductase 3,Thioredoxin reductase TR2,Trxr3,Txnrd3
EIAAB44614 14 kDa thioredoxin-related protein,Mouse,Mus musculus,Protein 42-9-9,Thioredoxin domain-containing protein 17,Thioredoxin-like protein 5,TRP14,Txndc17,Txnl5
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
EIAAB43736 Homo sapiens,Human,Protein TXNRD3NB,Thioredoxin reductase 2 intronic transcript 1,Thioredoxin reductase 3 intronic transcript 1,Thioredoxin reductase 3 neighbor gene protein,Thioredoxin reductase 3 ne
Mab-607057 Monoclonal Antibodies: Thioredoxin (TRX); Specificity: Thioredoxin (TRX) ; Application: IHC 0.1ml
EIAAB44633 Mouse,Mus musculus,Spermatid-specific thioredoxin-2,Sptrx2,Sptrx-2,Thioredoxin domain-containing protein 3,Txndc3


 

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