Recombinant Escherichia coli Blue copper oxidase CueO (cueO)

Code CSB-YP339713ENV
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Source Yeast
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Code CSB-EP339713ENV
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Source E.coli
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Code CSB-EP339713ENV-B
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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-BP339713ENV
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Source Baculovirus
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Code CSB-MP339713ENV
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
cueO
Uniprot No.
Alternative Names
cueO; yacK; b0123; JW0119Blue copper oxidase CueO; Copper efflux oxidase
Species
Escherichia coli (strain K12)
Expression Region
29-516
Target Protein Sequence
AE RPTLPIPDLL TTDARNRIQL TIGAGQSTFG GKTATTWGYN GNLLGPAVKL QRGKAVTVDI YNQLTEETTL HWHGLEVPGE VDGGPQGIIP PGGKRSVTLN VDQPAATCWF HPHQHGKTGR QVAMGLAGLV VIEDDEILKL MLPKQWGIDD VPVIVQDKKF SADGQIDYQL DVMTAAVGWF GDTLLTNGAI YPQHAAPRGW LRLRLLNGCN ARSLNFATSD NRPLYVIASD GGLLPEPVKV SELPVLMGER FEVLVEVNDN KPFDLVTLPV SQMGMAIAPF DKPHPVMRIQ PIAISASGAL PDTLSSLPAL PSLEGLTVRK LQLSMDPMLD MMGMQMLMEK YGDQAMAGMD HSQMMGHMGH GNMNHMNHGG KFDFHHANKI NGQAFDMNKP MFAAAKGQYE RWVISGVGDM MLHPFHIHGT QFRILSENGK PPAAHRAGWK DTVKVEGNVS EVLVKFNHDA PKEHAYMAHC HLLEHEDTGM MLGFTV
Protein Length
Full Length of Mature Protein
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.

Customer Reviews and Q&A

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Target Background

Function
Probably involved in periplasmic detoxification of copper by oxidizing Cu(+) to Cu(2+) and thus preventing its uptake into the cytoplasm. Possesses phenoloxidase and ferroxidase activities and might be involved in the production of polyphenolic compounds and the prevention of oxidative damage in the periplasm.
Gene References into Functions
  1. Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO has been presented. PMID: 27710945
  2. Exogenous acetate ion reaches the type II copper center in CueO through the water-excretion channel and potentially affects the enzymatic activity. PMID: 27380373
  3. the binding of copper to apo-CueO greatly stabilized the protein, indicating a transformation from an open or flexible domain arrangement with accessible copper sites to a closed structure with deeply buried copper ions. PMID: 27129241
  4. The results provides evidence that CueO possesses high Mn(II) oxidase activity and generates biogenic Mn oxide gamma-Mn3O4. PMID: 24699422
  5. At low levels of X-ray exposure, unambiguous electron density for an O atom is observed inside the trinuclear copper center (TNC); binding of oxygen to the TNC after its full reduction is observed in the case of the laccase. PMID: 24598746
  6. Laccase activities of CueO were maximally enhanced 140-fold by virtue of the synergistic effect of mild mutations at and at around the ligand groups to type I copper. PMID: 23337502
  7. These results exerted on the hydrogen bond network in CueO are discussed in comparison with proton transfers in cytochrome oxidase. PMID: 22564733
  8. The results revealed that the crude CueO catalyzed the oxidation of anthracene and benzo[a]pyrene in the same way as the fungal laccase from Trametes versicolor, but showed specific characteristics such as thermostability and copper dependence. PMID: 21120471
  9. has robust cuprous oxidase activity which is central to the mechanism by which CueO protects E coli against copper toxicity PMID: 15516598
  10. Copper toxicity towards a cueO mutant could be suppressed by addition of the superoxide quencher 1,2-dihydroxybenzene-3,5-disulfonic acid (tiron), suggesting that a primary cause of copper toxicity is the copper-catalyzed production of superoxide anions. PMID: 15708004
  11. Transcriptional profiling showed that expression of genes associated with motility was lowered in a cueO mutant while expression of genes associated with autoaggregation was elevated. PMID: 17635554
  12. Data indicate that the methionine-rich alpha-helices of CueO function as a barrier to the access of bulky organic substrates, which provides CueO with specificity as a cuprous oxidase. PMID: 17804014

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Subcellular Location
Periplasm. Note=It is exported via the Tat pathway.
Protein Families
Multicopper oxidase family
Database Links
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