Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

SUOX

Uniprot No.

P51687

Research Area

Metabolism

Alternative Names

EC 1.8.3.1; mitochondrial; Sulfite oxidase; Sulfite oxidase mitochondrial ; Sulfite oxidase; mitochondrial precursor; Suox; SUOX_HUMAN

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

80-545aa

Target Protein Sequence

ESTHIYTKEEVSSHTSPETGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPLEPFWALYAVHNQSHVRELLAQYKIGELNPEDKVAPTVETSDPYADDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEAHVCFEGLDSDPTGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQRPRKAWAWRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYVSP
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

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.

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.

Troubleshooting and FAQs

Protein 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

3-7 business days

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.

Description

The region for expressing recombinant Human SUOX contains amino acids 80-545. This SUOX protein is expected to have a theoretical molecular weight of 67.6 kDa. The SUOX protein was expressed in e.coli. The SUOX coding gene included the N-terminal 6xHis-SUMO tag, which simplifies the detection and purification processes of the recombinant SUOX protein in following stages of expression and purification.

Sulfite oxidase, mitochondrial (SUOX) is a crucial enzyme involved in the oxidation of sulfite to sulfate in the mitochondria. This process is vital for the metabolism of sulfur-containing amino acids, such as cysteine and methionine. SUOX plays a pivotal role in maintaining sulfur homeostasis and preventing the accumulation of toxic sulfite levels in the body. Additionally, SUOX is essential for the proper functioning of the molybdenum cofactor (Moco), a prosthetic group required for the enzyme's activity. Mutations in the SUOX gene can lead to a rare inherited disorder known as isolated sulfite oxidase deficiency, characterized by neurological abnormalities and other health complications. Research on SUOX contributes to a better understanding of sulfur metabolism, redox balance, and the molecular basis of genetic disorders related to sulfite oxidase deficiency.

Target Background

Gene References into Functions

SUOX is negatively associated with the progression and proliferation of oral squamous cell carcinoma. PMID: 29280012
This is the first description of the prenatal neurodevelopment of brain disruption in isolated sulfite oxidase deficiency. PMID: 28629418
Novel SUOX mutations were detected in 3 Sulfite oxidase deficiency cases PMID: 27289259
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
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
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
SUOX was decreased and AKR1B10 and CD34 were increased with the stepwise progression of hepatocarcinogenesis. PMID: 23665285
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
effect of mutation of surface residues on the heme domain on intramolecular electron transfer, and steady-state kinetics PMID: 22975842
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
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
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
role of conserved tyrosine 343 in intramolecular electron transfer in this enzyme PMID: 12424234
Sulfite oxidase gene expression in brain and in other tissues. PMID: 12763039
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
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
the Tyr(343) residue is important for both substrate binding and oxidation of sulfite by sulfite oxidase PMID: 14729666
mutation in SUOX gene in sulfite oxidase deficiency PMID: 16140720
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
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
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
analysis of protein-protein interaction of sulfite oxidase and cytochrome c catalyzing oxidation of sulfite PMID: 18177044
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
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

Code	CSB-EP022954HU
Abbreviation	Recombinant Human SUOX protein
MSDS	MSDS Datasheet
Size	$224
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Recombinant Human Sulfite oxidase, mitochondrial (SUOX)

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