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Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)

 SODC_MOUSE              Reviewed;         154 AA.
P08228;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 202.
RecName: Full=Superoxide dismutase [Cu-Zn];
EC=1.15.1.1;
Name=Sod1;
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=SWR/J; TISSUE=Liver;
PubMed=3362683; DOI=10.1093/nar/16.6.2728;
Bewley G.C.;
"cDNA and deduced amino acid sequence of murine Cu-Zn superoxide
dismutase.";
Nucleic Acids Res. 16:2728-2728(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2022332; DOI=10.1016/0378-1119(91)90126-V;
Benedetto M.T., Anzai Y., Gordon J.W.;
"Isolation and analysis of the mouse genomic sequence encoding Cu(2+)-
Zn2+ superoxide dismutase.";
Gene 99:191-195(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Ovary, Urinary bladder, and Uterus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Liver, Mammary gland, and Retina;
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).
[5]
PROTEIN SEQUENCE OF 4-23.
PubMed=2391363; DOI=10.1083/jcb.111.3.1217;
Pluthero F.G., Shreeve M., Eskinazi D., van der Gaag H., Huang K.S.,
Hulmes J.D., Blum M., Axelrad A.A.;
"Purification of an inhibitor of erythroid progenitor cell cycling and
antagonist to interleukin 3 from mouse marrow cell supernatants and
its identification as cytosolic superoxide dismutase.";
J. Cell Biol. 111:1217-1223(1990).
[6]
PROTEIN SEQUENCE OF 11-24 AND 104-116, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Klug S., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, 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).
[8]
DISRUPTION PHENOTYPE.
TISSUE=Liver;
PubMed=21420488; DOI=10.1016/j.freeradbiomed.2011.03.018;
Wang S.K., Weaver J.D., Zhang S., Lei X.G.;
"Knockout of SOD1 promotes conversion of selenocysteine to
dehydroalanine in murine hepatic GPX1 protein.";
Free Radic. Biol. Med. 51:197-204(2011).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-123, SUCCINYLATION
[LARGE SCALE ANALYSIS] AT LYS-4; LYS-10; LYS-92; LYS-123 AND LYS-137,
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).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, 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).
[11]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC.
PubMed=20727846; DOI=10.1016/j.abb.2010.08.014;
Seetharaman S.V., Taylor A.B., Holloway S., Hart P.J.;
"Structures of mouse SOD1 and human/mouse SOD1 chimeras.";
Arch. Biochem. Biophys. 503:183-190(2010).
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
Note=Binds 1 copper ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20727846}.
-!- INTERACTION:
P99029:Prdx5; NbExp=2; IntAct=EBI-1635090, EBI-2735704;
P63001:Rac1; NbExp=4; IntAct=EBI-1635090, EBI-413646;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
-!- PTM: Palmitoylation helps nuclear targeting and decreases
catalytic activity. {ECO:0000250}.
-!- PTM: Succinylation, adjacent to copper catalytic site, probably
inhibits activity. Desuccinylation by SIRT5 enhances activity.
{ECO:0000250|UniProtKB:P00441}.
-!- DISRUPTION PHENOTYPE: 40% reduction in hepatic GPX1 activity.
{ECO:0000269|PubMed:21420488}.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
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EMBL; X06683; CAA29880.1; -; mRNA.
EMBL; M60798; AAA40121.1; -; Genomic_DNA.
EMBL; M60794; AAA40121.1; JOINED; Genomic_DNA.
EMBL; M60795; AAA40121.1; JOINED; Genomic_DNA.
EMBL; M60796; AAA40121.1; JOINED; Genomic_DNA.
EMBL; M60797; AAA40121.1; JOINED; Genomic_DNA.
EMBL; M35725; AAA37518.1; -; mRNA.
EMBL; AK020624; BAB32154.1; -; mRNA.
EMBL; AK077284; BAC36730.1; -; mRNA.
EMBL; BC002066; AAH02066.1; -; mRNA.
EMBL; BC048874; AAH48874.1; -; mRNA.
EMBL; BC086886; AAH86886.1; -; mRNA.
CCDS; CCDS37395.1; -.
PIR; JQ0915; JQ0915.
RefSeq; NP_035564.1; NM_011434.1.
UniGene; Mm.276325; -.
UniGene; Mm.466779; -.
PDB; 3GTT; X-ray; 2.40 A; A/B/C/D/E/F=2-154.
PDB; 3GTV; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=82-154.
PDB; 3LTV; X-ray; 2.45 A; A/B/C/D/E/F=2-81.
PDBsum; 3GTT; -.
PDBsum; 3GTV; -.
PDBsum; 3LTV; -.
ProteinModelPortal; P08228; -.
SMR; P08228; -.
BioGrid; 203387; 29.
ComplexPortal; CPX-2898; [Cu-Zn] Superoxide dismutase complex.
DIP; DIP-48691N; -.
IntAct; P08228; 53.
MINT; P08228; -.
STRING; 10090.ENSMUSP00000023707; -.
iPTMnet; P08228; -.
PhosphoSitePlus; P08228; -.
SwissPalm; P08228; -.
DOSAC-COBS-2DPAGE; P08228; -.
REPRODUCTION-2DPAGE; IPI00130589; -.
REPRODUCTION-2DPAGE; P08228; -.
SWISS-2DPAGE; P08228; -.
UCD-2DPAGE; P08228; -.
EPD; P08228; -.
MaxQB; P08228; -.
PaxDb; P08228; -.
PeptideAtlas; P08228; -.
PRIDE; P08228; -.
Ensembl; ENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.
GeneID; 20655; -.
KEGG; mmu:20655; -.
UCSC; uc007zvz.1; mouse.
CTD; 6647; -.
MGI; MGI:98351; Sod1.
eggNOG; KOG0441; Eukaryota.
eggNOG; COG2032; LUCA.
GeneTree; ENSGT00530000063226; -.
HOGENOM; HOG000263447; -.
HOVERGEN; HBG000062; -.
InParanoid; P08228; -.
KO; K04565; -.
OMA; IHTFGDN; -.
OrthoDB; EOG091G0OG2; -.
PhylomeDB; P08228; -.
TreeFam; TF105131; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
ChiTaRS; Sod1; mouse.
EvolutionaryTrace; P08228; -.
PRO; PR:P08228; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022982; Expressed in 306 organ(s), highest expression level in cumulus cell.
CleanEx; MM_SOD1; -.
Genevisible; P08228; MM.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
GO; GO:0031045; C:dense core granule; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005777; C:peroxisome; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0030141; C:secretory granule; ISO:MGI.
GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; ISO:MGI.
GO; GO:0004784; F:superoxide dismutase activity; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IDA:MGI.
GO; GO:0007568; P:aging; IMP:MGI.
GO; GO:0008089; P:anterograde axonal transport; IMP:BHF-UCL.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
GO; GO:0007569; P:cell aging; ISO:MGI.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:MGI.
GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0035865; P:cellular response to potassium ion; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IMP:MGI.
GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
GO; GO:0060047; P:heart contraction; IMP:MGI.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
GO; GO:0002262; P:myeloid cell homeostasis; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI.
GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0060087; P:relaxation of vascular smooth muscle; IMP:MGI.
GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0097332; P:response to antipsychotic drug; IEA:Ensembl.
GO; GO:0048678; P:response to axon injury; IMP:MGI.
GO; GO:0034465; P:response to carbon monoxide; IEA:Ensembl.
GO; GO:0046688; P:response to copper ion; ISO:MGI.
GO; GO:0042493; P:response to drug; IMP:MGI.
GO; GO:0045471; P:response to ethanol; IMP:MGI.
GO; GO:0009408; P:response to heat; IMP:MGI.
GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
GO; GO:0031667; P:response to nutrient levels; ISO:MGI.
GO; GO:0010033; P:response to organic substance; ISS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
GO; GO:0000303; P:response to superoxide; IMP:MGI.
GO; GO:0001895; P:retina homeostasis; IMP:MGI.
GO; GO:0008090; P:retrograde axonal transport; IMP:BHF-UCL.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0042554; P:superoxide anion generation; IDA:MGI.
GO; GO:0006801; P:superoxide metabolic process; IMP:MGI.
GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR018152; SOD_Cu/Zn_BS.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00080; Sod_Cu; 1.
PRINTS; PR00068; CUZNDISMTASE.
SUPFAM; SSF49329; SSF49329; 1.
PROSITE; PS00087; SOD_CU_ZN_1; 1.
PROSITE; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antioxidant; Complete proteome; Copper;
Cytoplasm; Direct protein sequencing; Disulfide bond; Lipoprotein;
Metal-binding; Nucleus; Oxidoreductase; Palmitate; Phosphoprotein;
Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:23806337}.
CHAIN 2 154 Superoxide dismutase [Cu-Zn].
/FTId=PRO_0000164062.
METAL 47 47 Copper; catalytic. {ECO:0000250}.
METAL 49 49 Copper; catalytic. {ECO:0000250}.
METAL 64 64 Copper; catalytic. {ECO:0000250}.
METAL 64 64 Zinc; via pros nitrogen.
{ECO:0000269|PubMed:20727846}.
METAL 72 72 Zinc; via pros nitrogen.
{ECO:0000269|PubMed:20727846}.
METAL 81 81 Zinc; via pros nitrogen.
{ECO:0000269|PubMed:20727846}.
METAL 84 84 Zinc; structural.
{ECO:0000269|PubMed:20727846}.
METAL 121 121 Copper; catalytic. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 4 4 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 10 10 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 92 92 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000250|UniProtKB:P07632}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 123 123 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 123 123 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 137 137 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 137 137 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
LIPID 7 7 S-palmitoyl cysteine. {ECO:0000250}.
DISULFID 58 147 {ECO:0000250}.
CONFLICT 102 102 D -> H (in Ref. 2; AAA40121).
{ECO:0000305}.
STRAND 3 10 {ECO:0000244|PDB:3GTT}.
STRAND 12 14 {ECO:0000244|PDB:3GTT}.
STRAND 16 25 {ECO:0000244|PDB:3GTT}.
STRAND 30 38 {ECO:0000244|PDB:3GTT}.
STRAND 41 50 {ECO:0000244|PDB:3GTT}.
TURN 55 58 {ECO:0000244|PDB:3GTT}.
HELIX 59 61 {ECO:0000244|PDB:3GTT}.
STRAND 77 79 {ECO:0000244|PDB:3LTV}.
STRAND 84 90 {ECO:0000244|PDB:3GTT}.
STRAND 96 109 {ECO:0000244|PDB:3GTV}.
STRAND 116 123 {ECO:0000244|PDB:3GTV}.
STRAND 130 132 {ECO:0000244|PDB:3GTV}.
HELIX 133 138 {ECO:0000244|PDB:3GTV}.
STRAND 143 149 {ECO:0000244|PDB:3GTV}.
SEQUENCE 154 AA; 15943 MW; CAE548C66043BAC4 CRC64;
MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ YGDNTQGCTS
AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI EDRVISLSGE HSIIGRTMVV
HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAQ


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orb81377 Human Superoxide Dismutase-1 protein Recombinant Human Cu_Zn Superoxide Dismutase produced in E.coli is a single monomeric non-glycosylated polypeptide chain containing 154 amino acids and having tota 5
LF-MA0065 anti-Superoxide Dismutase 2 (4F10) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
LF-MA0019 anti-Superoxide Dismutase 4 (11G1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG1, Host Mouse 100 ul
LF-MA0023 anti-Superoxide Dismutase 1 (72B1), Mouse monoclonal to Superoxide Dismutase 1, Isotype IgG1, Host Mouse 100 ul
LF-MA0121 anti-Superoxide Dismutase 3 (1H12), Mouse monoclonal to Superoxide Dismutase 3, Isotype IgG2b, Host Mouse 100 ul
LF-MA0066 anti-Superoxide Dismutase 2 (23G5) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
SCH-MCA2595 MOUSE ANTI SUPEROXIDE DISMUTASE (Cu_Zn), Product Type Monoclonal Antibody, Specificity SUPEROXIDE DISMUTASE , Target Species Bovine, Host Mouse, Format Purified, Isotypes IgG1, Applications C, 0.1 mg
MCA2595 MOUSE ANTI SUPEROXIDE DISMUTASE (Cu_Zn), Product Type Monoclonal Antibody, Specificity SUPEROXIDE DISMUTASE , Target Species Bovine, Host Mouse, Format Purified, Isotypes IgG1, Applications C, 0.1 mg
LF-MA0030 anti-Superoxide Dismutase 2 (2A1), Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
LF-MA0035 anti-Superoxide Dismutase 2 (1E8) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG2b, Host Mouse 100 ul
LF-MA0016 anti-Superoxide Dismutase 4 (2A1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG1, Host Mouse 100 ul
LF-MA0042 anti-Superoxide Dismutase 4 (3A1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG2a, Host Mouse 100 ul
LF-MA0029 anti-Superoxide Dismutase 1 (8A1), Mouse monoclonal to Superoxide Dismutase 1, Isotype IgG1, Host Mouse 100 ul
LF-PA10015 anti-Superoxide Dismutase 2, Mouse polyclonal to Superoxide Dismutase 2, Isotype , Host Mouse 50 ug
LF-PA0021 anti-Superoxide Dismutase 2, Rabbit polyclonal to Superoxide Dismutase 2, Isotype IgG, Host Rabbit 100 ul
LF-PA0013 anti-Superoxide Dismutase 1, Rabbit polyclonal to Superoxide Dismutase 1, Isotype IgG, Host Rabbit 100 ul
orb80178 Human Superoxide Dismutase (homodimer) protein Recombinant Human Cu_Zn Superoxide Dismutase produced in E.coli is homodimer, non-glycosylated polypeptide chain containing 2x 154 amino acids and having 100
8475-0204 NATIVE BOVINE SUPEROXIDE DISMUTASE, Product Type Purified Protein, Specificity SUPEROXIDE DISMUTASE, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 100 KU
SCH-8475-0204 NATIVE BOVINE SUPEROXIDE DISMUTASE, Product Type Purified Protein, Specificity SUPEROXIDE DISMUTASE, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 100 KU


 

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