Gene Symbol | SOD1 |
Entrez Gene ID | 281495 |
Full Name | superoxide dismutase 1 |
Synonyms | SOD1L1 |
Gene Type | protein-coding |
Organism | Bos taurus(cattle) |
Genome |
ORF » Species Summary » Bos taurus » SOD1 cDNA ORF clone
Gene Symbol | SOD1 |
Entrez Gene ID | 281495 |
Full Name | superoxide dismutase 1 |
Synonyms | SOD1L1 |
Gene Type | protein-coding |
Organism | Bos taurus(cattle) |
Genome |
mRNA | Protein | Name |
---|---|---|
NM_174615.2 | NP_777040.1 | superoxide dismutase [Cu-Zn] |
Canis lupus familiaris (dog) | SOD1 | NP_001003035.1 |
Gallus gallus (chicken) | SOD1 | NP_990395.1 |
Anopheles gambiae (African malaria mosquito) | CUSOD3 | XP_311594.2 |
Mus musculus (house mouse) | Sod1 | NP_035564.1 |
Caenorhabditis elegans (roundworm) | sod-5 | NP_494779.1 |
Schizosaccharomyces pombe (fission yeast) | sod1 | NP_593163.1 |
Homo sapiens (human) | SOD1 | NP_000445.1 |
Pan troglodytes (chimpanzee) | SOD1 | NP_001009025.1 |
SOD1 | NP_001027976.1 | |
Rattus norvegicus (Norway rat) | Sod1 | NP_058746.1 |
Caenorhabditis elegans (roundworm) | sod-1 | NP_001021956.1 |
Xenopus tropicalis (tropical clawed frog) | sod1 | NP_001016252.1 |
Bos taurus (cattle) | SOD1 | NP_777040.1 |
Saccharomyces cerevisiae (baker's yeast) | SOD1 | NP_012638.1 |
Kluyveromyces lactis | KLLA0E05567g | XP_454197.1 |
Magnaporthe oryzae (rice blast fungus) | MGG_02625 | XP_003721165.1 |
Arabidopsis thaliana (thale cress) | CSD1 | NP_001077494.1 |
Danio rerio (zebrafish) | sod1 | NP_571369.1 |
Drosophila melanogaster (fruit fly) | Sod | NP_001261700.1 |
Eremothecium gossypii | AGOS_AGL321W | NP_986346.2 |
Neurospora crassa | NCU02133 | XP_964291.2 |
Oryza sativa (rice) | Os03g0351500 | NP_001050118.1 |
Oryza sativa (rice) | Os07g0665200 | NP_001060564.1 |
Distinct oxidative cleavage and modification of bovine [Cu- Zn]-SOD by an ascorbic acid/Cu(II) system: Identification of novel copper binding site on SOD molecule.
Uehara H, Luo S, Aryal B, Levine RL, Rao VA
Free radical biology & medicine94161-73(2016 05)
New insights of superoxide dismutase inhibition of pyrogallol autoxidation.
Ramasarma T, Rao AV, Devi MM, Omkumar RV, Bhagyashree KS, Bhat SV
Molecular and cellular biochemistry400(1-2)277-85(2015 Feb)
GeneRIFs: Gene References Into Functions What's a GeneRIF?
The three-dimensional structure of bSOD1 reveals the imidazole ring of His19 localized within 5A from the alpha-carbon of Gly31 providing a structural basis that copper ion, most likely coordinated by His19, catalyzes the specific cleavage reaction
Title: Distinct oxidative cleavage and modification of bovine [Cu- Zn]-SOD by an ascorbic acid/Cu(II) system: Identification of novel copper binding site on SOD molecule.
SOD catalyzes reversal of autoxidation manifesting as its inhibition. SOD saves catechols from autoxidation and extends their bioavailability
Title: New insights of superoxide dismutase inhibition of pyrogallol autoxidation.
antioxidative enzymatic mechanisms in bovine placental tissues are represented by superoxide dismutase 1 and glutathione peroxidase, which show the changes in their expression during improper placental release
Title: The presence of SOD 1 and GSH-Px in bovine retained and properly released foetal membranes.
Results sugget thet Copper/Zinc superoxide dismutase (SOD1) may play a role in controlling intraluteal prostaglandin F2alph and reactive oxygen species action during functional and structural luteolysis.
Title: Roles of prostaglandin F2alpha and hydrogen peroxide in the regulation of Copper/Zinc superoxide dismutase in bovine corpus luteum and luteal endothelial cells.
At room temperature (25.0 degrees C) and higher, the addition of high concentrations of polymer is found to significantly enhance the affinity of SOD for catalase.
Title: Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria.
The following SOD1 gene cDNA ORF clone sequences were retrieved from the NCBI Reference Sequence Database (RefSeq). These sequences represent the protein coding region of the SOD1 cDNA ORF which is encoded by the open reading frame (ORF) sequence. ORF sequences can be delivered in our standard vector, pcDNA3.1+/C-(K)DYK or the vector of your choice as an expression/transfection-ready ORF clone. Not the clone you want? Click here to find your clone.
CloneID | OBa01220 | |
Clone ID Related Accession (Same CDS sequence) | NM_174615.2 | |
Accession Version | NM_174615.2 Latest version! | Documents for ORF clone product in default vector |
Sequence Information | ORF Nucleotide Sequence (Length: 459bp) Protein sequence SNP |
|
Vector | pcDNA3.1-C-(k)DYK or customized vector | User Manual |
Clone information | Clone Map | MSDS |
Tag on pcDNA3.1+/C-(K)DYK | C terminal DYKDDDDK tags | |
ORF Insert Method | CloneEZ™ Seamless cloning technology | |
Insert Structure | linear | |
Update Date | 2019-10-18 | |
Organism | Bos taurus(cattle) | |
Product | superoxide dismutase [Cu-Zn] | |
Comment | Comment: PROVISIONAL REFSEQ: This record has not yet been subject to final NCBI review. The reference sequence was derived from M81129.1. On Jun 3, 2003 this sequence version replaced NM_174615.1. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: M81129.1, BC102432.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN03145412, SAMN03145413 [ECO:0000348] ##Evidence-Data-END## |
1 | ATGGCGACGA AGGCCGTCTG CGTGCTGAAG GGCGACGGCC CGGTGCAAGG CACCATCCAC |
The stop codons will be deleted if pcDNA3.1+/C-(K)DYK vector is selected.
RefSeq | NP_777040.1 |
CDS | 80..538 |
Translation |
Target ORF information:
Target ORF information:
|
NM_174615.2 |
1 | ATGGCGACGA AGGCCGTCTG CGTGCTGAAG GGCGACGGCC CGGTGCAAGG CACCATCCAC |
The stop codons will be deleted if pcDNA3.1+/C-(K)DYK vector is selected.
Distinct oxidative cleavage and modification of bovine [Cu- Zn]-SOD by an ascorbic acid/Cu(II) system: Identification of novel copper binding site on SOD molecule. |
New insights of superoxide dismutase inhibition of pyrogallol autoxidation. |