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

Catalase (EC 1.11.1.6)

 CATA_MOUSE              Reviewed;         527 AA.
P24270; Q3TXQ6;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
20-DEC-2017, entry version 167.
RecName: Full=Catalase;
EC=1.11.1.6;
Name=Cat; Synonyms=Cas-1, Cas1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/CS(A); TISSUE=Kidney, and Liver;
PubMed=2268310; DOI=10.1016/S0006-291X(05)80891-5;
Shaffer J.B., Preston K.E.;
"Molecular analysis of an acatalasemic mouse mutant.";
Biochem. Biophys. Res. Commun. 173:1043-1050(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/CS(A), and C3H/HeJ; TISSUE=Liver;
PubMed=2395665; DOI=10.1093/nar/18.16.4941;
Shaffer J.B., Preston K.E., Shepard B.A.;
"Nucleotide and deduced amino acid sequences of mouse catalase:
molecular analysis of a low activity mutant.";
Nucleic Acids Res. 18:4941-4941(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=8088826; DOI=10.1006/geno.1994.1273;
Reimer D.L., Bailley J., Singh S.M.;
"Complete cDNA and 5' genomic sequences and multilevel regulation of
the mouse catalase gene.";
Genomics 21:325-336(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Amnion, and Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
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).
[8]
PROTEIN SEQUENCE OF 2-12; 221-232; 287-300; 306-314 AND 468-475,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
Kanor S., Quadroni M., Bienvenut W.V.;
Submitted (MAR-2006) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 48-66, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 503-527.
PubMed=3654595;
Shaffer J.B., Sutton R.B., Bewley G.C.;
"Isolation of a cDNA clone for murine catalase and analysis of an
acatalasemic mutant.";
J. Biol. Chem. 262:12908-12911(1987).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-422 AND SER-517,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
"Mitochondrial phosphoproteome revealed by an improved IMAC method and
MS/MS/MS.";
Mol. Cell. Proteomics 6:669-676(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-434, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-434 AND SER-517,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-449, SUCCINYLATION
[LARGE SCALE ANALYSIS] AT LYS-13; LYS-221; LYS-306; LYS-430; LYS-449;
LYS-480 AND LYS-522, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast, and Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233; LYS-306; LYS-430;
LYS-449; LYS-480 AND LYS-499, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- FUNCTION: Occurs in almost all aerobically respiring organisms and
serves to protect cells from the toxic effects of hydrogen
peroxide. Promotes growth of cells.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|PROSITE-ProRule:PRU10013}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- COFACTOR:
Name=NADP(+); Xref=ChEBI:CHEBI:58349;
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Peroxisome.
-!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M62897; AAA37373.1; -; mRNA.
EMBL; X52108; CAA36342.1; -; mRNA.
EMBL; L25069; AAA66054.1; -; mRNA.
EMBL; AK150893; BAE29939.1; -; mRNA.
EMBL; AK159152; BAE34859.1; -; mRNA.
EMBL; AK159885; BAE35454.1; -; mRNA.
EMBL; AK159891; BAE35458.1; -; mRNA.
EMBL; AK169069; BAE40856.1; -; mRNA.
EMBL; AL773505; CAM17512.1; -; Genomic_DNA.
EMBL; CH466519; EDL27697.1; -; Genomic_DNA.
EMBL; BC013447; AAH13447.1; -; mRNA.
EMBL; M29394; AAA37371.1; -; mRNA.
CCDS; CCDS16478.1; -.
PIR; A36695; A36695.
RefSeq; NP_033934.2; NM_009804.2.
UniGene; Mm.4215; -.
ProteinModelPortal; P24270; -.
SMR; P24270; -.
BioGrid; 198490; 2.
IntAct; P24270; 3.
MINT; MINT-1859622; -.
STRING; 10090.ENSMUSP00000028610; -.
iPTMnet; P24270; -.
PhosphoSitePlus; P24270; -.
SwissPalm; P24270; -.
SWISS-2DPAGE; P24270; -.
EPD; P24270; -.
MaxQB; P24270; -.
PaxDb; P24270; -.
PeptideAtlas; P24270; -.
PRIDE; P24270; -.
Ensembl; ENSMUST00000028610; ENSMUSP00000028610; ENSMUSG00000027187.
GeneID; 12359; -.
KEGG; mmu:12359; -.
UCSC; uc008liw.2; mouse.
CTD; 847; -.
MGI; MGI:88271; Cat.
eggNOG; KOG0047; Eukaryota.
eggNOG; COG0753; LUCA.
GeneTree; ENSGT00390000018100; -.
HOGENOM; HOG000087852; -.
HOVERGEN; HBG003986; -.
InParanoid; P24270; -.
KO; K03781; -.
OMA; HADFGRM; -.
OrthoDB; EOG091G04V5; -.
TreeFam; TF300540; -.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Cat; mouse.
PRO; PR:P24270; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027187; -.
CleanEx; MM_CAT; -.
ExpressionAtlas; P24270; baseline and differential.
Genevisible; P24270; MM.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005764; C:lysosome; IEA:Ensembl.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005778; C:peroxisomal membrane; IDA:MGI.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0004046; F:aminoacylase activity; IMP:MGI.
GO; GO:0016209; F:antioxidant activity; ISO:MGI.
GO; GO:0004096; F:catalase activity; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0020037; F:heme binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050661; F:NADP binding; ISO:MGI.
GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0009060; P:aerobic respiration; IMP:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
GO; GO:0020027; P:hemoglobin metabolic process; IMP:MGI.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:MGI.
GO; GO:0001649; P:osteoblast differentiation; ISO:MGI.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:MGI.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0051262; P:protein tetramerization; ISO:MGI.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0014854; P:response to inactivity; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0009642; P:response to light intensity; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
GO; GO:0010193; P:response to ozone; IEA:Ensembl.
GO; GO:0080184; P:response to phenylpropanoid; IEA:Ensembl.
GO; GO:0000302; P:response to reactive oxygen species; ISO:MGI.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
GO; GO:0009650; P:UV protection; ISO:MGI.
Gene3D; 2.40.180.10; -; 1.
InterPro; IPR018028; Catalase.
InterPro; IPR024708; Catalase_AS.
InterPro; IPR024711; Catalase_clade1/3.
InterPro; IPR011614; Catalase_core.
InterPro; IPR037060; Catalase_core_sf.
InterPro; IPR002226; Catalase_haem_BS.
InterPro; IPR010582; Catalase_immune_responsive.
InterPro; IPR020835; Catalase_sf.
PANTHER; PTHR11465; PTHR11465; 1.
Pfam; PF00199; Catalase; 1.
Pfam; PF06628; Catalase-rel; 1.
PIRSF; PIRSF038928; Catalase_clade1-3; 1.
PRINTS; PR00067; CATALASE.
SMART; SM01060; Catalase; 1.
SUPFAM; SSF56634; SSF56634; 1.
PROSITE; PS00437; CATALASE_1; 1.
PROSITE; PS00438; CATALASE_2; 1.
PROSITE; PS51402; CATALASE_3; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing; Heme;
Hydrogen peroxide; Iron; Metal-binding; Mitogen; NADP; Oxidoreductase;
Peroxidase; Peroxisome; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:23806337,
ECO:0000269|Ref.8}.
CHAIN 2 527 Catalase.
/FTId=PRO_0000084902.
ACT_SITE 75 75 {ECO:0000255|PROSITE-ProRule:PRU10013}.
ACT_SITE 148 148 {ECO:0000255|PROSITE-ProRule:PRU10013}.
METAL 358 358 Iron (heme axial ligand). {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:23806337,
ECO:0000269|Ref.8}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000250|UniProtKB:P04040}.
MOD_RES 13 13 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:17208939,
ECO:0000244|PubMed:21183079}.
MOD_RES 221 221 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 233 233 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 306 306 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 306 306 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:17208939}.
MOD_RES 430 430 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 430 430 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 449 449 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337}.
MOD_RES 449 449 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 480 480 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 480 480 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 499 499 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 511 511 Phosphothreonine.
{ECO:0000250|UniProtKB:P04040}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000244|PubMed:17208939,
ECO:0000244|PubMed:21183079}.
MOD_RES 522 522 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MUTAGEN 11 11 Q->H: Acatalasemia.
CONFLICT 97 97 A -> G (in Ref. 3; AAA66054).
{ECO:0000305}.
CONFLICT 117 117 T -> A (in Ref. 1; AAA37373, 2; CAA36342,
3; AAA66054 and 4; AAH13447).
{ECO:0000305}.
CONFLICT 316 316 L -> V (in Ref. 3; AAA66054).
{ECO:0000305}.
CONFLICT 350 350 M -> K (in Ref. 3; AAA66054).
{ECO:0000305}.
SEQUENCE 527 AA; 59795 MW; 4D86F3C9D1A3DF9E CRC64;
MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL LVQDVVFTDE
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVTGES
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNADGEAV YCKFHYKTDQ
GIKNLPVGEA GRLAQEDPDY GLRDLFNAIA NGNYPSWTFY IQVMTFKEAE TFPFNPFDLT
KVWPHKDYPL IPVGKLVLNK NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD
THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG APNYYPNSFS APEQQRSALE
HSVQCAVDVK RFNSANEDNV TQVRTFYTKV LNEEERKRLC ENIAGHLKDA QLFIQKKAVK
NFTDVHPDYG ARIQALLDKY NAEKPKNAIH TYTQAGSHMA AKGKANL


Related products :

Catalog number Product name Quantity
AS09 501 Antibody: Cat | Catalase, Immunogen: KLH-conjugated peptide chosen from know plant catalase sequences including Arabidopsis thaliana isoforms: catalase-1 (Q96528, At1g20630), catalase-2 (P25819, At4g3 200
ECAT-100 EnzyChrom™ Catalase Assay Kit, Quantitative determination of catalase activity by colorimetric (570nm) or fluorometric (530nm_590nm) methods 100Tests
3806BP-50 Catalase Blocking Peptide target: Catalase 50 μg
3806BP-50 Catalase Blocking Peptide Catalase 50 μg
ECAT-100 EnzyChrom™ Catalase Assay Kit, Quantitative determination of catalase activity by colorimetric (570nm) or fluorometric (530nm_590nm) methods. Procedure 40 min. Kit size 100 tests. Detection limit 0 100tests
LF-MA0010 anti-Catalase (11A1), Mouse monoclonal to Catalase, Isotype IgG2a, Host Mouse 100 ul
LF-MA0004 anti-Catalase (2A1), Mouse monoclonal to Catalase, Isotype IgG1, Host Mouse 100 ul
LF-MA10386 anti-Catalase, Mouse monoclonal to Catalase, Isotype IgG2a , Host Mouse 100 ug
LF-MA0003 anti-Catalase (1A1), Mouse monoclonal to Catalase, Isotype IgG2b, Host Mouse 100 ul
LF-PA40204 anti-Catalase, Rabbit polyclonal to Catalase, Isotype IgG, Host Rabbit 50 ug
LF-PA10005 anti-Catalase, Mouse polyclonal to Catalase, Isotype , Host Mouse 50 uL
LF-PA10006 anti-Catalase, Mouse polyclonal to Catalase, Isotype , Host Mouse 50 ug
LF-PA0060 anti-Catalase, Rabbit polyclonal to Catalase, Isotype IgG, Host Rabbit 100 ul
LF-PA0218 anti-Catalase, Rabbit polyclonal to Catalase, Isotype IgG, Host Rabbit 100 ul
9001-05-2 Catalase Catalase 1g
1890-0010 SHEEP ANTI BOVINE CATALASE, Product Type Polyclonal Antibody, Specificity CATALASE, Target Species Bovine, Host Sheep, Format Purified, Isotypes Polyclonal IgG, Applications C, E, Clone 1 ml
SCH-1890-0010 SHEEP ANTI BOVINE CATALASE, Product Type Polyclonal Antibody, Specificity CATALASE, Target Species Bovine, Host Sheep, Format Purified, Isotypes Polyclonal IgG, Applications C, E, Clone 1 ml
MCA4785Z MOUSE ANTI HUMAN CATALASE Azide free, Product Type Monoclonal Antibody, Specificity CATALASE, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2a, Applications WB, Clone 2G6 0.1 mg
18-272-197004 Catalase - Peroxisome Marker - Rabbit polyclonal to Catalase - Peroxisome Marker Polyclonal 1 ml
70-720 CAT _ Catalase Antibody 0.05 mg
187-10.TH CATALASE, Bovine 10 kU
Y104435 Catalase Bv 1 ml
187-10.2X CATALASE, Bovine 25 kU
Y104318 Catalase 1 ml
000490A Catalase 250ul


 

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