Recombinant Human Sulfite oxidase, mitochondrial(SUOX)

Code CSB-EP022954HU
Size US$1726
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names SUOX
Uniprot No. P51687
Research Area Metabolism
Alternative Names EC; mitochondrial; Sulfite oxidase; Sulfite oxidase mitochondrial ; Sulfite oxidase; mitochondrial precursor; Suox; SUOX_HUMAN
Species Homo sapiens (Human)
Source E.coli
Expression Region 80-545aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 67.6kDa
Protein Length Full Length of Mature Protein
Tag Info N-terminal 6xHis-SUMO-tagged
Form Liquid or 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 If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is 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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°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.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Gene References into Functions
  1. SUOX is negatively associated with the progression and proliferation of oral squamous cell carcinoma. PMID: 29280012
  2. This is the first description of the prenatal neurodevelopment of brain disruption in isolated sulfite oxidase deficiency. PMID: 28629418
  3. Novel SUOX mutations were detected in 3 Sulfite oxidase deficiency cases PMID: 27289259
  4. Nitrite binds and reduces at the molybdenum site of mammalian sulfite oxidase, which may be allosterically regulated by heme and molybdenum domain interactions, and contributes to the mammalian nitrate-nitrite-NO signaling pathway in human fibroblasts. PMID: 25314640
  5. This finding suggests the possibility to use oxygen-reactive SO variants in sulfite detoxification, as the loss of SO activity is causing severe neurodegeneration PMID: 26171830
  6. Several mutants of H304 and R309 of SUOX were investigated by steady-state kinetics, laser flash photolysis studies of intramolecular electron transfer (IET), and spectroelectrochemistry. PMID: 24968320
  7. SUOX was decreased and AKR1B10 and CD34 were increased with the stepwise progression of hepatocarcinogenesis. PMID: 23665285
  8. combined genetic association studies in women from China/Netherlands/United States: Data suggest that an SNP in SUOX locus (rs705702) and SNPs in other proteins are associated with polycystic ovary syndrome across ethnic differences. [META-ANALYSIS] PMID: 24106282
  9. effect of mutation of surface residues on the heme domain on intramolecular electron transfer, and steady-state kinetics PMID: 22975842
  10. In this study a human sulfite oxidase variant, in which the active site has been modified to alter substrate specificity and activity from sulfite oxidation to nitrate reduction, is compared to chicken sulfite oxidase. PMID: 22263579
  11. prepared and purified samples of the wild type and various mutants of human SO that are depleted of chloride. These samples do not exhibit the typical lpH EPR spectrum at low pH but rather exhibit spectra that are characteristic of the blocked species PMID: 20491442
  12. Experimental deletions of nonconserved amino acids in the 14-residue interdomain polypeptide tether of sulfite oxidase shorten its length and result in more drastically reduced intramolecular electron transfer rate constants. PMID: 20063894
  13. role of conserved tyrosine 343 in intramolecular electron transfer in this enzyme PMID: 12424234
  14. Sulfite oxidase gene expression in brain and in other tissues. PMID: 12763039
  15. comparison of this structure with other b(5)-type cytochromes reveals distinct structural features present in the sulfite oxidase b(5) domain which promote optimal electron transport between the Moco of sulfite oxidase and the heme of cytochrome c PMID: 12832761
  16. To further assess the role of Arg 160 in human SO, intramolecular electron transfer rates between the reduced heme and oxidized molybdenum centers in the wild type, R160Q, and R160K human SO forms were investigated by laser flash photolysis PMID: 14567685
  17. the Tyr(343) residue is important for both substrate binding and oxidation of sulfite by sulfite oxidase PMID: 14729666
  18. mutation in SUOX gene in sulfite oxidase deficiency PMID: 16140720
  19. mutations to charged residues at the equivalent sites most likely cause crucial global or localized structural changes, and expose an alternative docking site that may compete with the Mo domain for docking of the heme PMID: 16229463
  20. Analysis of recombinant G473D sulfite oxidase indicated that it is severely impaired both in the ability to bind sulfite and in catalysis, with a second-order rate constant 5 orders of magnitude lower than that of the wild type. PMID: 16475804
  21. Magnetic resonance imaging and MR spectroscopy measurements may help differentiate isolated sulfite oxidase deficiency from hypoxic-ischemic condition in patients in whom this diagnosis is not clinically suspected. PMID: 17940249
  22. analysis of protein-protein interaction of sulfite oxidase and cytochrome c catalyzing oxidation of sulfite PMID: 18177044
  23. EPR study of the Mo(V) center of the pathogenic R160Q mutant confirms the presence of three distinct species whose relative abundances depend upon pH. PMID: 18529001
  24. the activity of molybdoenzymes, such as sulfite oxidase, is inhibited by high concentrations of heavy metals in the cell PMID: 18959753

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Involvement in disease Isolated sulfite oxidase deficiency (ISOD)
Subcellular Location Mitochondrion intermembrane space
Database Links

HGNC: 11460

OMIM: 272300

KEGG: hsa:6821

STRING: 9606.ENSP00000266971

UniGene: Hs.558403

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