Recombinant Human Sulfite Oxidase, Mitochondrial (SUOX) Protein (His)

Name: Recombinant Human Sulfite Oxidase, Mitochondrial (SUOX) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09714P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Sulfite Oxidase, Mitochondrial (SUOX) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P51687
Target Symbol	SUOX
Synonyms	EC 1.8.3.1; mitochondrial; Sulfite oxidase; Sulfite oxidase mitochondrial ; Sulfite oxidase; mitochondrial precursor; Suox; SUOX_HUMAN
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	ESTHIYTKEEVSSHTSPETGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPLEPFWALYAVHNQSHVRELLAQYKIGELNPEDKVAPTVETSDPYADDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEAHVCFEGLDSDPTGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQRPRKAWAWRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYVSP
Expression Range	80-545aa
Protein Length	Full Length of Mature Protein
Mol. Weight	53.6kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Subcellular Location	Mitochondrion intermembrane space.
Database References	HGNC: 11460 OMIM: 272300 KEGG: hsa:6821 STRING: 9606.ENSP00000266971 UniGene: Hs.558403
Associated Diseases	Isolated sulfite oxidase deficiency (ISOD)

Gene Functions References

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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.