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

Peroxiredoxin-1 (EC 1.11.1.15) (HBP23) (Heme-binding 23 kDa protein) (Thioredoxin peroxidase 2) (Thioredoxin-dependent peroxide reductase 2)

 PRDX1_RAT               Reviewed;         199 AA.
Q63716;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 151.
RecName: Full=Peroxiredoxin-1;
EC=1.11.1.15;
AltName: Full=HBP23;
AltName: Full=Heme-binding 23 kDa protein;
AltName: Full=Thioredoxin peroxidase 2;
AltName: Full=Thioredoxin-dependent peroxide reductase 2;
Name=Prdx1; Synonyms=Tdpx2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=7577926; DOI=10.1021/bi00041a017;
Iwahara S., Satoh H., Song D.-X., Webb J., Burlingame A.L., Nagae Y.,
Mueller-Eberhard U.;
"Purification, characterization, and cloning of a heme-binding protein
(23 kDa) in rat liver cytosol.";
Biochemistry 34:13398-13406(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver, and Pituitary;
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).
[3]
PROTEIN SEQUENCE OF 17-35 AND 111-190, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[4]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN OXIDIZED FORM, AND DISULFIDE
BONDS.
PubMed=10535922; DOI=10.1073/pnas.96.22.12333;
Hirotsu S., Abe Y., Okada K., Nagahara N., Hori H., Nishino T.,
Hakoshima T.;
"Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-
binding protein 23 kDa/proliferation-associated gene product.";
Proc. Natl. Acad. Sci. U.S.A. 96:12333-12338(1999).
[5]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), DISULFIDE BONDS, AND CATALYTIC
ACTIVITY.
PubMed=17974571; DOI=10.1074/jbc.M705753200;
Matsumura T., Okamoto K., Iwahara S., Hori H., Takahashi Y.,
Nishino T., Abe Y.;
"Dimer-oligomer interconversion of wild-type and mutant rat 2-Cys
peroxiredoxin: disulfide formation at dimer-dimer interfaces is not
essential for decamerization.";
J. Biol. Chem. 283:284-293(2008).
-!- 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. Might participate in
the signaling cascades of growth factors and tumor necrosis
factor-alpha by regulating the intracellular concentrations of
H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond
in GDPD5 that gates the ability to GDPD5 to drive postmitotic
motor neuron differentiation (By similarity).
{ECO:0000250|UniProtKB:P0CB50, ECO:0000250|UniProtKB:Q06830}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000250|UniProtKB:Q06830}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation
(PubMed:10535922). 5 homodimers assemble to form a ring-like
decamer (PubMed:17974571). Interacts with GDPD5; forms a mixed-
disulfide with GDPD5 (By similarity). Interacts with SESN1 and
SESN2 (By similarity). {ECO:0000250|UniProtKB:P0CB50,
ECO:0000250|UniProtKB:Q06830, ECO:0000269|PubMed:10535922,
ECO:0000269|PubMed:17974571}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06830}.
-!- PTM: Phosphorylated on Thr-90 during the M-phase, which leads to a
decrease in enzymatic activity. {ECO:0000250|UniProtKB:Q06830}.
-!- 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:10535922}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D30035; BAA06275.1; -; mRNA.
EMBL; BC058450; AAH58450.1; -; mRNA.
EMBL; BC088118; AAH88118.1; -; mRNA.
PIR; I52425; I52425.
RefSeq; NP_476455.1; NM_057114.1.
UniGene; Rn.2845; -.
PDB; 1QQ2; X-ray; 2.60 A; A/B=1-199.
PDB; 2Z9S; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=1-199.
PDBsum; 1QQ2; -.
PDBsum; 2Z9S; -.
ProteinModelPortal; Q63716; -.
SMR; Q63716; -.
BioGrid; 250701; 3.
IntAct; Q63716; 5.
STRING; 10116.ENSRNOP00000023132; -.
PeroxiBase; 4508; Rno2CysPrx01.
iPTMnet; Q63716; -.
PhosphoSitePlus; Q63716; -.
SwissPalm; Q63716; -.
World-2DPAGE; 0004:Q63716; -.
PaxDb; Q63716; -.
PRIDE; Q63716; -.
Ensembl; ENSRNOT00000023132; ENSRNOP00000023132; ENSRNOG00000017194.
GeneID; 117254; -.
KEGG; rno:117254; -.
UCSC; RGD:620039; rat.
CTD; 5052; -.
RGD; 620039; Prdx1.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00390000004653; -.
HOGENOM; HOG000022343; -.
HOVERGEN; HBG000286; -.
InParanoid; Q63716; -.
KO; K13279; -.
OMA; FAWTNTP; -.
OrthoDB; EOG091G0IE5; -.
PhylomeDB; Q63716; -.
TreeFam; TF105181; -.
BRENDA; 1.11.1.15; 5301.
Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
EvolutionaryTrace; Q63716; -.
PRO; PR:Q63716; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000017194; -.
Genevisible; Q63716; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
GO; GO:0005719; C:nuclear euchromatin; IDA:RGD.
GO; GO:0005730; C:nucleolus; IDA:RGD.
GO; GO:0005782; C:peroxisomal matrix; IDA:RGD.
GO; GO:0020037; F:heme binding; IPI:RGD.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0051920; F:peroxiredoxin activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
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; 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:0000250|UniProtKB:Q06830}.
CHAIN 2 199 Peroxiredoxin-1.
/FTId=PRO_0000135078.
DOMAIN 6 165 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 52 52 Cysteine sulfenic acid (-SOH)
intermediate.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q06830}.
MOD_RES 7 7 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q06830}.
MOD_RES 16 16 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q06830}.
MOD_RES 27 27 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q06830}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000250|UniProtKB:Q06830}.
MOD_RES 35 35 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q06830}.
MOD_RES 35 35 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P35700}.
MOD_RES 90 90 Phosphothreonine.
{ECO:0000250|UniProtKB:Q06830}.
MOD_RES 136 136 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35700}.
DISULFID 52 52 Interchain (with C-173); in linked form.
{ECO:0000244|PDB:1QQ2,
ECO:0000269|PubMed:10535922,
ECO:0000269|PubMed:17974571}.
DISULFID 173 173 Interchain (with C-52); in linked form.
{ECO:0000244|PDB:1QQ2,
ECO:0000269|PubMed:10535922,
ECO:0000269|PubMed:17974571}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q06830}.
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q06830}.
CROSSLNK 185 185 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q06830}.
STRAND 16 20 {ECO:0000244|PDB:1QQ2}.
STRAND 26 30 {ECO:0000244|PDB:1QQ2}.
HELIX 31 34 {ECO:0000244|PDB:1QQ2}.
STRAND 37 43 {ECO:0000244|PDB:1QQ2}.
STRAND 50 52 {ECO:0000244|PDB:1QQ2}.
HELIX 57 61 {ECO:0000244|PDB:1QQ2}.
HELIX 63 68 {ECO:0000244|PDB:1QQ2}.
STRAND 71 78 {ECO:0000244|PDB:1QQ2}.
HELIX 81 88 {ECO:0000244|PDB:1QQ2}.
HELIX 92 94 {ECO:0000244|PDB:1QQ2}.
STRAND 104 106 {ECO:0000244|PDB:1QQ2}.
HELIX 111 115 {ECO:0000244|PDB:1QQ2}.
STRAND 121 124 {ECO:0000244|PDB:1QQ2}.
STRAND 128 133 {ECO:0000244|PDB:1QQ2}.
STRAND 137 145 {ECO:0000244|PDB:1QQ2}.
HELIX 153 168 {ECO:0000244|PDB:1QQ2}.
STRAND 170 172 {ECO:0000244|PDB:1QQ2}.
TURN 188 191 {ECO:0000244|PDB:2Z9S}.
HELIX 192 195 {ECO:0000244|PDB:2Z9S}.
SEQUENCE 199 AA; 22109 MW; BDF2D4ABA8A776DA CRC64;
MSSGNAKIGH PAPSFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS
DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK
ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEILRLV QAFQFTDKHG EVCPAGWKPG
SDTIKPDVNK SKEYFSKQK


Related products :

Catalog number Product name Quantity
E2222r HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2
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 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 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 HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
EIAAB32327 Antioxidant enzyme AOE372,Mouse,Mus musculus,Peroxiredoxin IV,Peroxiredoxin-4,Prdx4,Prx-IV,Thioredoxin peroxidase AO372,Thioredoxin-dependent peroxide reductase A0372
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
U1123p CLIA Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
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
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 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
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
E1123r ELISA kit Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,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
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
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
E2222m ELISA kit 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 reducta 96T
U2222m CLIA kit 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 reductas 96T
E2222h Homo sapiens,Human,Natural killer cell-enhancing factor A,NKEF-A,PAG,PAGA,PAGB,Peroxiredoxin-1,PRDX1,Proliferation-associated gene protein,TDPX2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide


 

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