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

Peroxiredoxin-2C (EC 1.11.1.15) (Peroxiredoxin IIC) (Peroxiredoxin TPx2) (Thioredoxin peroxidase 2C) (Thioredoxin-dependent peroxidase 2)

 PRX2C_ARATH             Reviewed;         162 AA.
Q9SRZ4;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 117.
RecName: Full=Peroxiredoxin-2C;
EC=1.11.1.15 {ECO:0000269|Ref.7};
AltName: Full=Peroxiredoxin IIC;
AltName: Full=Peroxiredoxin TPx2;
AltName: Full=Thioredoxin peroxidase 2C;
AltName: Full=Thioredoxin-dependent peroxidase 2;
Name=PRXIIC; Synonyms=TPX2; OrderedLocusNames=At1g65970;
ORFNames=F12P19.13;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
SPECIFICITY, AND INDUCTION.
DOI=10.1016/S0981-9428(02)01396-7;
Horling F., Koenig J., Dietz K.-J.;
"Type II peroxiredoxin C, a member of the peroxiredoxin family of
Arabidopsis thaliana: its expression and activity in comparison with
other peroxiredoxins.";
Plant Physiol. Biochem. 40:491-499(2002).
[8]
INDUCTION.
PubMed=12529539; DOI=10.1104/pp.010017;
Horling F., Lamkemeyer P., Koenig J., Finkemeier I., Kandlbinder A.,
Baier M., Dietz K.-J.;
"Divergent light-, ascorbate-, and oxidative stress-dependent
regulation of expression of the peroxiredoxin gene family in
Arabidopsis.";
Plant Physiol. 131:317-325(2003).
[9]
TISSUE SPECIFICITY.
PubMed=12913160; DOI=10.1104/pp.103.022533;
Brehelin C., Meyer E.H., de Souris J.-P., Bonnard G., Meyer Y.;
"Resemblance and dissemblance of Arabidopsis type II peroxiredoxins:
similar sequences for divergent gene expression, protein localization,
and activity.";
Plant Physiol. 132:2045-2057(2003).
[10]
GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
PubMed=15890615; DOI=10.1016/j.freeradbiomed.2004.07.037;
Rouhier N., Jacquot J.-P.;
"The plant multigenic family of thiol peroxidases.";
Free Radic. Biol. Med. 38:1413-1421(2005).
-!- 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.
{ECO:0000305|PubMed:15890615}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|Ref.7}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Vmax=8.9 nmol/min/mg enzyme for H(2)O(2) {ECO:0000269|Ref.7};
-!- SUBUNIT: Monomer. {ECO:0000269|Ref.7}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in buds and flowers. Slightly
expressed in green tissues. Also detected in pollen.
{ECO:0000269|PubMed:12913160, ECO:0000269|Ref.7}.
-!- INDUCTION: Highly induced by salt or oxidative stresses.
{ECO:0000269|PubMed:12529539, ECO:0000269|Ref.7}.
-!- 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 1-Cys peroxiredoxin, no C(R) is present and C(P)
instead forms a disulfide with a cysteine from another protein or
with a small thiol molecule. {ECO:0000250|UniProtKB:A9PCL4}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF121356; AAD28243.1; -; mRNA.
EMBL; AC009513; AAF06057.1; -; Genomic_DNA.
EMBL; CP002684; AEE34446.1; -; Genomic_DNA.
EMBL; AF332463; AAG48826.1; -; mRNA.
EMBL; BT003050; AAO23615.1; -; mRNA.
EMBL; AY084458; AAM61030.1; -; mRNA.
EMBL; AK227350; BAE99360.1; -; mRNA.
PIR; A96684; A96684.
RefSeq; NP_176772.1; NM_105269.4.
UniGene; At.24993; -.
UniGene; At.66846; -.
ProteinModelPortal; Q9SRZ4; -.
SMR; Q9SRZ4; -.
STRING; 3702.AT1G65970.1; -.
PeroxiBase; 4347; AtPrxII03.
PaxDb; Q9SRZ4; -.
PRIDE; Q9SRZ4; -.
EnsemblPlants; AT1G65970.1; AT1G65970.1; AT1G65970.
GeneID; 842909; -.
Gramene; AT1G65970.1; AT1G65970.1; AT1G65970.
KEGG; ath:AT1G65970; -.
Araport; AT1G65970; -.
TAIR; locus:2009709; AT1G65970.
eggNOG; KOG0541; Eukaryota.
eggNOG; COG0678; LUCA.
HOGENOM; HOG000255884; -.
InParanoid; Q9SRZ4; -.
OMA; SCHANHL; -.
OrthoDB; EOG09360OQV; -.
PhylomeDB; Q9SRZ4; -.
BioCyc; ARA:AT1G65970-MONOMER; -.
PRO; PR:Q9SRZ4; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9SRZ4; baseline and differential.
Genevisible; Q9SRZ4; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
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;
Antioxidant; Complete proteome; Cytoplasm; Oxidoreductase; Peroxidase;
Redox-active center; Reference proteome.
CHAIN 1 162 Peroxiredoxin-2C.
/FTId=PRO_0000282280.
DOMAIN 4 162 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 51 51 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:A9PCL4}.
SEQUENCE 162 AA; 17414 MW; 7EEBEA0B56666E0A CRC64;
MAPITVGDVV PDGTISFFDE NDQLQTVSVH SIAAGKKVIL FGVPGAFTPT CSMSHVPGFI
GKAEELKSKG IDEIICFSVN DPFVMKAWGK TYPENKHVKF VADGSGEYTH LLGLELDLKD
KGLGIRSRRF ALLLDNLKVT VANVESGGEF TVSSAEDILK AL


Related products :

Catalog number Product name Quantity
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
E2222r HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2
E1123p ELISA kit Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123p ELISA 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
E1123r ELISA Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,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
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
U1123r CLIA Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,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
U1123m CLIA Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 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
E2222r ELISA HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
E1123m ELISA Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 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
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
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


 

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