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Transcriptional regulator URE2 (Disulfide reductase) (EC 1.8.4.-) (Glutathione peroxidase) (EC 1.11.1.9)

 URE2_YEAST              Reviewed;         354 AA.
P23202; D6W0W3;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
23-MAY-2018, entry version 177.
RecName: Full=Transcriptional regulator URE2;
AltName: Full=Disulfide reductase;
EC=1.8.4.-;
AltName: Full=Glutathione peroxidase;
EC=1.11.1.9;
Name=URE2; OrderedLocusNames=YNL229C; ORFNames=N1165;
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], AND FUNCTION.
PubMed=1990286; DOI=10.1128/MCB.11.2.822;
Coschigano P.W., Magasanik B.;
"The URE2 gene product of Saccharomyces cerevisiae plays an important
role in the cellular response to the nitrogen source and has homology
to glutathione s-transferases.";
Mol. Cell. Biol. 11:822-832(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 14085 / CBS 3093 / IFO 1997 / NRRL Y-12657,
ATCC 9804 / CBS 400 / DSM 70478 / IFO 0210 / JCM 2220, Boots,
CBS 2087, CBS 4734, CBS 5112, CBS 5287, CBS 7957,
Chevalieri / ATCC 10604 / CBS 405 / IFO 0258 / NRRL Y-1546,
Fleischmann, McPhie Sourdough, SAF, Sigma 1278B, Wyeast#1007, YJM 143,
YJM 280, YJM 320, YJM 326, and YJM 415;
PubMed=12177423; DOI=10.1073/pnas.162349599;
Edskes H.K., Wickner R.B.;
"Conservation of a portion of the S. cerevisiae Ure2p prion domain
that interacts with the full-length protein.";
Proc. Natl. Acad. Sci. U.S.A. 99:16384-16391(2002).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8896273;
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1071::AID-YEA4>3.3.CO;2-J;
Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
"The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
reading frames including a novel gene encoding a globin-like domain.";
Yeast 12:1071-1076(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[5]
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).
[6]
PRION FORMATION.
PubMed=7909170; DOI=10.1126/science.7909170;
Wickner R.B.;
"[URE3] as an altered URE2 protein: evidence for a prion analog in
Saccharomyces cerevisiae.";
Science 264:566-569(1994).
[7]
DOMAIN PRION.
PubMed=7569955; DOI=10.1126/science.270.5233.93;
Masison D.C., Wickner R.B.;
"Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p
in prion-containing cells.";
Science 270:93-95(1995).
[8]
FUNCTION.
PubMed=8755910; DOI=10.1128/jb.178.15.4734-4736.1996;
Blinder D., Coschigano P.W., Magasanik B.;
"Interaction of the GATA factor Gln3p with the nitrogen regulator
Ure2p in Saccharomyces cerevisiae.";
J. Bacteriol. 178:4734-4736(1996).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10604478; DOI=10.1038/45287;
Beck T., Hall M.N.;
"The TOR signalling pathway controls nuclear localization of nutrient-
regulated transcription factors.";
Nature 402:689-692(1999).
[10]
FUNCTION.
PubMed=10799523; DOI=10.1074/jbc.275.19.14408;
Cunningham T.S., Andhare R., Cooper T.G.;
"Nitrogen catabolite repression of DAL80 expression depends on the
relative levels of Gat1p and Ure2p production in Saccharomyces
cerevisiae.";
J. Biol. Chem. 275:14408-14414(2000).
[11]
PRION FORMATION, AND PRION CURING.
PubMed=11073991; DOI=10.1128/MCB.20.23.8916-8922.2000;
Moriyama H., Edskes H.K., Wickner R.B.;
"[URE3] prion propagation in Saccharomyces cerevisiae: requirement for
chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.";
Mol. Cell. Biol. 20:8916-8922(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]
FUNCTION.
PubMed=15371425; DOI=10.1074/jbc.M406612200;
Bai M., Zhou J.M., Perrett S.;
"The yeast prion protein Ure2 shows glutathione peroxidase activity in
both native and fibrillar forms.";
J. Biol. Chem. 279:50025-50030(2004).
[14]
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).
[15]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF ALA-122 AND ASN-124.
PubMed=19321443; DOI=10.1074/jbc.M901189200;
Zhang Z.R., Perrett S.;
"Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a
native-like dimer within fibrils.";
J. Biol. Chem. 284:14058-14067(2009).
[16]
INTERACTION WITH NNK1.
PubMed=20489023; DOI=10.1126/science.1176495;
Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V.,
Larsen B., Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J.,
Dewar-Darch D., Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T.,
Gingras A.C., Nesvizhskii A.I., Tyers M.;
"A global protein kinase and phosphatase interaction network in
yeast.";
Science 328:1043-1046(2010).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 95-354 IN COMPLEX WITH
GLUTATHIONE AND INHIBITORS.
PubMed=11695904; DOI=10.1021/bi011007b;
Bousset L., Belrhali H., Melki R., Morera S.;
"Crystal structures of the yeast prion Ure2p functional region in
complex with glutathione and related compounds.";
Biochemistry 40:13564-13573(2001).
[19]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 97-354.
PubMed=11171973; DOI=10.1073/pnas.98.4.1459;
Umland T.C., Taylor K.L., Rhee S., Wickner R.B., Davies D.R.;
"The crystal structure of the nitrogen regulation fragment of the
yeast prion protein Ure2p.";
Proc. Natl. Acad. Sci. U.S.A. 98:1459-1464(2001).
[20]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-353.
PubMed=11342133; DOI=10.1016/S0969-2126(00)00553-0;
Bousset L., Belrhali H., Janin J., Melki R., Morera S.;
"Structure of the globular region of the prion protein Ure2 from the
yeast Saccharomyces cerevisiae.";
Structure 9:39-46(2001).
[21]
STRUCTURE BY NMR OF 10-39.
PubMed=16060675; DOI=10.1021/bi050724t;
Chan J.C., Oyler N.A., Yau W.M., Tycko R.;
"Parallel beta-sheets and polar zippers in amyloid fibrils formed by
residues 10-39 of the yeast prion protein Ure2p.";
Biochemistry 44:10669-10680(2005).
[22]
STRUCTURE BY NMR OF 1-89, AND DOMAIN PRION.
PubMed=17953455; DOI=10.1021/bi700826b;
Baxa U., Wickner R.B., Steven A.C., Anderson D.E., Marekov L.N.,
Yau W.M., Tycko R.;
"Characterization of beta-sheet structure in Ure2p(1-89) yeast prion
fibrils by solid-state nuclear magnetic resonance.";
Biochemistry 46:13149-13162(2007).
-!- FUNCTION: Plays an important role in nitrogen catabolite
repression. Down-regulates the expression of many genes involved
in nitrogen utilization by inhibiting the GATA transcriptional
activators GLN3 and GAT1. Under good nitrogen conditions, binds to
the phosphorylated forms of GLN3 and GAT1 and sequesters them in
the cytoplasm, preventing transcription of genes expressed upon
nitrogen limitation. Is also an atypical glutaredoxin without a
catalytical cysteine residue. Has glutathione peroxidase and
thiol:disulfide oxidoreductase activities in both native and
fibrillar form. Also shows insulin disulfide reductase and
dehydroascorbic acid reductase (DHAR) actvites.
{ECO:0000269|PubMed:10604478, ECO:0000269|PubMed:10799523,
ECO:0000269|PubMed:15371425, ECO:0000269|PubMed:19321443,
ECO:0000269|PubMed:1990286, ECO:0000269|PubMed:8755910}.
-!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
disulfide + 2 H(2)O. {ECO:0000269|PubMed:19321443}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.4 mM for bis-(2-hydroxyethyl) disulfide (HEDS)
{ECO:0000269|PubMed:19321443};
Note=kcat is 1.2 sec(-1) with bis-(2-hydroxyethyl) disulfide
(HEDS) as substrate.;
-!- SUBUNIT: Homodimer. Interacts with NNK1.
{ECO:0000269|PubMed:11695904, ECO:0000269|PubMed:20489023}.
-!- INTERACTION:
P18494:GLN3; NbExp=2; IntAct=EBI-20138, EBI-7657;
P36003:NNK1; NbExp=4; IntAct=EBI-20138, EBI-9796;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10604478}.
-!- DOMAIN: The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain,
which is unstructured in its native, soluble form, and which forms
a parallel in-register beta-sheet in its amyloid form.
{ECO:0000269|PubMed:17953455, ECO:0000269|PubMed:7569955}.
-!- MISCELLANEOUS: [URE3] is the prion form of URE2. [URE3] is the
result of a conformational change of the cellular URE2 protein
that becomes self-propagating and infectious. This conformational
change generates a form of URE2 that assembles into amyloid
fibrils. [URE3]-aggregates sequester soluble URE2, which then
fails to retain GLN3 in the cytoplasm, resulting in GLN3
activation and consequently derepression of genes that are
required for utilization of poor nirogen sources (PubMed:7909170).
[URE3] can be cured by GdnHCl and by deletion of the molecular
chaperone HSP104, which is required for [URE3] propagation
(PubMed:11073991). {ECO:0000305|PubMed:11073991,
ECO:0000305|PubMed:7909170}.
-!- MISCELLANEOUS: Present with 7060 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Mad yeast disease
- Issue 47 of June 2004;
URL="https://web.expasy.org/spotlight/back_issues/047";
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EMBL; M35268; AAA35201.1; -; Genomic_DNA.
EMBL; AF525174; AAM93167.1; -; Genomic_DNA.
EMBL; AF525175; AAM93168.1; -; Genomic_DNA.
EMBL; AF525176; AAM93169.1; -; Genomic_DNA.
EMBL; AF525177; AAM93170.1; -; Genomic_DNA.
EMBL; AF525178; AAM93171.1; -; Genomic_DNA.
EMBL; AF525179; AAM93172.1; -; Genomic_DNA.
EMBL; AF525180; AAM93173.1; -; Genomic_DNA.
EMBL; AF525181; AAM93174.1; -; Genomic_DNA.
EMBL; AF525182; AAM93175.1; -; Genomic_DNA.
EMBL; AF525183; AAM93176.1; -; Genomic_DNA.
EMBL; AF525184; AAM93177.1; -; Genomic_DNA.
EMBL; AF525185; AAM93178.1; -; Genomic_DNA.
EMBL; AF525186; AAM93179.1; -; Genomic_DNA.
EMBL; AF525187; AAM93180.1; -; Genomic_DNA.
EMBL; AF525188; AAM93181.1; -; Genomic_DNA.
EMBL; AF525189; AAM93182.1; -; Genomic_DNA.
EMBL; AF525190; AAM93183.1; -; Genomic_DNA.
EMBL; AF525191; AAM93184.1; -; Genomic_DNA.
EMBL; AF525192; AAM93185.1; -; Genomic_DNA.
EMBL; Z69381; CAA93369.1; -; Genomic_DNA.
EMBL; Z71505; CAA96134.1; -; Genomic_DNA.
EMBL; BK006947; DAA10329.1; -; Genomic_DNA.
PIR; A39609; A39609.
RefSeq; NP_014170.1; NM_001183067.1.
PDB; 1G6W; X-ray; 2.50 A; A/B/C/D=94-354.
PDB; 1G6Y; X-ray; 2.80 A; A/B=94-354.
PDB; 1HQO; X-ray; 2.30 A; A/B=97-354.
PDB; 1JZR; X-ray; 2.90 A; A/B/C/D=95-354.
PDB; 1K0A; X-ray; 2.50 A; A/B=95-354.
PDB; 1K0B; X-ray; 2.50 A; A/B/C/D=95-354.
PDB; 1K0C; X-ray; 2.50 A; A/B/C/D=95-354.
PDB; 1K0D; X-ray; 2.20 A; A/B/C/D=95-354.
PDBsum; 1G6W; -.
PDBsum; 1G6Y; -.
PDBsum; 1HQO; -.
PDBsum; 1JZR; -.
PDBsum; 1K0A; -.
PDBsum; 1K0B; -.
PDBsum; 1K0C; -.
PDBsum; 1K0D; -.
DisProt; DP00353; -.
ProteinModelPortal; P23202; -.
SMR; P23202; -.
BioGrid; 35609; 342.
DIP; DIP-1308N; -.
IntAct; P23202; 33.
MINT; P23202; -.
STRING; 4932.YNL229C; -.
MoonProt; P23202; -.
iPTMnet; P23202; -.
MaxQB; P23202; -.
PaxDb; P23202; -.
PRIDE; P23202; -.
EnsemblFungi; YNL229C; YNL229C; YNL229C.
GeneID; 855492; -.
KEGG; sce:YNL229C; -.
EuPathDB; FungiDB:YNL229C; -.
SGD; S000005173; URE2.
HOGENOM; HOG000125742; -.
InParanoid; P23202; -.
KO; K00799; -.
OMA; TIFLDFN; -.
OrthoDB; EOG092C499E; -.
BioCyc; YEAST:YNL229C-MONOMER; -.
EvolutionaryTrace; P23202; -.
PRO; PR:P23202; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:SGD.
GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
GO; GO:0051219; F:phosphoprotein binding; IDA:SGD.
GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IMP:SGD.
GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
GO; GO:0032447; P:protein urmylation; IMP:SGD.
GO; GO:0006808; P:regulation of nitrogen utilization; IMP:SGD.
GO; GO:0010044; P:response to aluminum ion; IMP:SGD.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017298; Ure2.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
PIRSF; PIRSF037861; Prion_URE2; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Amyloid; Complete proteome; Cytoplasm;
Nitrate assimilation; Oxidoreductase; Prion; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 354 Transcriptional regulator URE2.
/FTId=PRO_0000186013.
DOMAIN 112 196 GST N-terminal.
DOMAIN 205 354 GST C-terminal.
REGION 2 89 Prion domain (PrD).
REGION 164 165 Glutathione binding.
REGION 180 181 Glutathione binding.
BINDING 124 124 Glutathione.
{ECO:0000269|PubMed:11695904}.
BINDING 151 151 Glutathione.
{ECO:0000269|PubMed:11695904}.
MOD_RES 2 2 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MUTAGEN 122 122 A->S: Reduces glutaredoxin activity.
{ECO:0000269|PubMed:19321443}.
MUTAGEN 124 124 N->A,V: Abolishes glutaredoxin activity.
{ECO:0000269|PubMed:19321443}.
MUTAGEN 313 313 F->S: Destroys protein function.
HELIX 101 105 {ECO:0000244|PDB:1K0D}.
STRAND 111 118 {ECO:0000244|PDB:1K0D}.
HELIX 123 134 {ECO:0000244|PDB:1K0D}.
STRAND 139 143 {ECO:0000244|PDB:1K0D}.
TURN 146 149 {ECO:0000244|PDB:1K0D}.
HELIX 150 152 {ECO:0000244|PDB:1K0D}.
HELIX 154 157 {ECO:0000244|PDB:1K0D}.
STRAND 167 170 {ECO:0000244|PDB:1K0D}.
TURN 171 175 {ECO:0000244|PDB:1K0D}.
STRAND 176 180 {ECO:0000244|PDB:1K0D}.
HELIX 181 196 {ECO:0000244|PDB:1K0D}.
HELIX 206 222 {ECO:0000244|PDB:1K0D}.
HELIX 224 235 {ECO:0000244|PDB:1K0D}.
STRAND 237 239 {ECO:0000244|PDB:1G6W}.
HELIX 242 271 {ECO:0000244|PDB:1K0D}.
TURN 276 278 {ECO:0000244|PDB:1K0B}.
HELIX 279 284 {ECO:0000244|PDB:1G6W}.
STRAND 285 287 {ECO:0000244|PDB:1G6W}.
HELIX 289 291 {ECO:0000244|PDB:1G6W}.
HELIX 293 295 {ECO:0000244|PDB:1G6W}.
HELIX 308 311 {ECO:0000244|PDB:1K0D}.
HELIX 314 317 {ECO:0000244|PDB:1K0D}.
HELIX 320 323 {ECO:0000244|PDB:1K0D}.
HELIX 327 330 {ECO:0000244|PDB:1K0D}.
HELIX 332 342 {ECO:0000244|PDB:1K0D}.
HELIX 345 350 {ECO:0000244|PDB:1K0D}.
SEQUENCE 354 AA; 40271 MW; 2C628976034B0F1C CRC64;
MMNNNGNQVS NLSNALRQVN IGNRNSNTTT DQSNINFEFS TGVNNNNNNN SSSNNNNVQN
NNSGRNGSQN NDNENNIKNT LEQHRQQQQA FSDMSHVEYS RITKFFQEQP LEGYTLFSHR
SAPNGFKVAI VLSELGFHYN TIFLDFNLGE HRAPEFVSVN PNARVPALID HGMDNLSIWE
SGAILLHLVN KYYKETGNPL LWSDDLADQS QINAWLFFQT SGHAPMIGQA LHFRYFHSQK
IASAVERYTD EVRRVYGVVE MALAERREAL VMELDTENAA AYSAGTTPMS QSRFFDYPVW
LVGDKLTIAD LAFVPWNNVV DRIGINIKIE FPEVYKWTKH MMRRPAVIKA LRGE


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K3009-1 Glutathione Reductase Fluorescent Kit Glutathione reductase (GR) plays an indirect but essential role in the prevention of oxidative damage within the cell by helping to maintain appropriate levels o 96 rxns
E0295b ELISA kit Bos taurus,Bovine,Cellular glutathione peroxidase,Glutathione peroxidase 1,GPX1,GPx-1,GSHPx-1 96T
E0295b ELISA Bos taurus,Bovine,Cellular glutathione peroxidase,Glutathione peroxidase 1,GPX1,GPx-1,GSHPx-1 96T
U0295m CLIA Cellular glutathione peroxidase,Glutathione peroxidase 1,Gpx1,GPx-1,GSHPx-1,Mouse,Mus musculus 96T
E0295m ELISA Cellular glutathione peroxidase,Glutathione peroxidase 1,Gpx1,GPx-1,GSHPx-1,Mouse,Mus musculus 96T
E0295r ELISA kit Cellular glutathione peroxidase,Glutathione peroxidase 1,Gpx1,GPx-1,GSHPx-1,Rat,Rattus norvegicus 96T
E0295r ELISA Cellular glutathione peroxidase,Glutathione peroxidase 1,Gpx1,GPx-1,GSHPx-1,Rat,Rattus norvegicus 96T
E0295m ELISA kit Cellular glutathione peroxidase,Glutathione peroxidase 1,Gpx1,GPx-1,GSHPx-1,Mouse,Mus musculus 96T
U0295b CLIA Bos taurus,Bovine,Cellular glutathione peroxidase,Glutathione peroxidase 1,GPX1,GPx-1,GSHPx-1 96T
U0295r CLIA Cellular glutathione peroxidase,Glutathione peroxidase 1,Gpx1,GPx-1,GSHPx-1,Rat,Rattus norvegicus 96T
U0295p CLIA Cellular glutathione peroxidase,Glutathione peroxidase 1,GPX1,GPx-1,GSHPx-1,Pig,Sus scrofa 96T
E0295p ELISA Cellular glutathione peroxidase,Glutathione peroxidase 1,GPX1,GPx-1,GSHPx-1,Pig,Sus scrofa 96T
E0295p ELISA kit Cellular glutathione peroxidase,Glutathione peroxidase 1,GPX1,GPx-1,GSHPx-1,Pig,Sus scrofa 96T
31-156 v-ets erythroblastosis virus E26 oncogene like isoform 2 (ERG) is a transcriptional regulator. It may participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransfer 0.1 mg
27-118 v-ets erythroblastosis virus E26 oncogene like isoform 2 (ERG) is a transcriptional regulator. It may participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransfer 0.05 mg


 

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