Recombinant Bovine Superoxide dismutase [Cu-Zn] (SOD1), partial

Code CSB-YP022397BO
MSDS
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Source Yeast
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Code CSB-EP022397BO
MSDS
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Source E.coli
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Code CSB-EP022397BO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP022397BO
MSDS
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Source Baculovirus
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Code CSB-MP022397BO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
SOD1
Uniprot No.
Alternative Names
SOD1; Superoxide dismutase [Cu-Zn]; EC 1.15.1.1
Species
Bos taurus (Bovine)
Expression Region
-
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Gene References into Functions
  1. Results indicate that variants of the PRLH and SOD1 genes are associated with heat tolerance in Chinese cattle. PMID: 30079537
  2. 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 PMID: 26872685
  3. SOD catalyzes reversal of autoxidation manifesting as its inhibition. SOD saves catechols from autoxidation and extends their bioavailability PMID: 25416864
  4. 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 PMID: 23398331
  5. 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. PMID: 23101731
  6. ALOX5AP, CPNE3, IL1R2, IL6, TLR2, TLR4, and THY1 were upregulated in blood polymorphonuclear cells in negative energy balance versus positive energy balance cows. PMID: 20072847
  7. Acute elevation of SOD may represent a response of luteal endothelial cells to protect themselves against oxidative stress induced by PGF during functional luteolysis. PMID: 20519832
  8. 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. PMID: 20682270
  9. Capillary electrophoresis and mass spectrometry to study the different structures of bovine SOD-1. In both cases, an average molecular mass corresponding to the apo-monomer SOD-1 was calculated. PMID: 20411580
  10. flexibility of the metal sites involved in present a single-crystal X-ray diffraction study of Cu,Zn superoxide dismutase in space group P212121 at 0.57 GPa. The crystal structure (hpSOD) was determined and refined at 2 A degrees resolution. PMID: 20516618
  11. expression profile in follicles: oocytes (SOD1 throughout ooplasm & nucleoplasm); cumulus cells (no SOD1 detected); granulosa cells (expressed SOD1); follicular fluid (small follicles show increased amounts of SOD1 in comparison with large follicles) PMID: 20197373
  12. Bovine erythrocyte Cu,Zn-superoxide dismutase (BESOD) is a dimeric enzyme composed of identical subunits associated through unusually strong non-covalent interactions. PMID: 14688234
  13. Raman spectrum analysis strongly suggests that the His41-mediated hydrogen bond bridge of Cu-Zn superoxide dismutase plays a crucial role in keeping the protein structure suitable for highly efficient catalytic reactions. PMID: 15096035
  14. HCO(3)(-)-derived oxidant does not alter significantly the Cu(II) active site geometry and histidine coordination to Cu(II) in SOD1 as does H(2)O(2) alone PMID: 15123612
  15. copper- and carbonate radical anion-mediated oxidations have roles in hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation PMID: 15607903
  16. SOD1 mutants gain fatty acid binding abilities based on their structural instability and form cytotoxic granular aggregates PMID: 15799963
  17. The kinetics of thermal dissociation of superoxide dismutase (SOD) was studied in 0.05 M Tris-HCl buffer at pH 7.4 containing 10(-4) M EDTA. PMID: 16202231
  18. Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). PMID: 17042490
  19. communication between the two monomers of SOD1 such that the binding of one zinc ion per homodimer has a more profound effect on the homodimeric protein structure than the binding of subsequent metal ions PMID: 17381088
  20. DNA accelerates the formation of SOD1 aggregates and is incorporated into SOD1 aggregates. SOD1 association with DNA, driven by electrostatic interactions, can restrict the orientation of SOD1 molecules and increase a SOD1 population along DNA strands. PMID: 17469801
  21. The results suggest that under cellular conditions ( approximately 5 mM bicarbonate) zinc-deficient SOD1 peroxidation could play a pathogenic role in neurodegenerative diseases. PMID: 17729118
  22. The expression of SOD1 and SOD2 through the course of the estrous cycle is reported. PMID: 18572235
  23. diminished hepatic protein nitration in the SOD1-/- mice was not directly related to plasma nitrite and nitrate concentrations PMID: 18573333
  24. DNAs tested are simultaneously condensed into a nanoparticle with a specific morphology during SOD1 aggregation, revealing that SOD1 aggregation and DNA condensation are two concurrent phenomena. PMID: 18690666
  25. Peroxymonocarbonate (HOOCO(2)(-)) is a key intermediate in the SOD1 peroxidase cycle and identify this species as the precursor of carbonate radical anions. PMID: 19286663

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Subcellular Location
Cytoplasm. Nucleus.
Protein Families
Cu-Zn superoxide dismutase family
Database Links
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