SUOX Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
---|---|
Primary Accession | P51687 |
Other Accession | Q60HD0, NP_001027559.1, NP_001027558.1 |
Reactivity | Human |
Predicted | Monkey |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 60283 Da |
Antigen Region | 160-187 aa |
Gene ID | 6821 |
---|---|
Other Names | Sulfite oxidase, mitochondrial, SUOX |
Target/Specificity | This SUOX antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 160-187 amino acids from the Central region of human SUOX. |
Dilution | WB~~1:1000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | SUOX Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | SUOX |
---|---|
Function | Catalyzes the oxidation of sulfite to sulfate, the terminal reaction in the oxidative degradation of sulfur-containing amino acids. |
Cellular Location | Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q07116} |
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Provided below are standard protocols that you may find useful for product applications.
Background
Sulfite oxidase is a homodimeric protein localized to the intermembrane space of mitochondria. Each subunit contains a heme domain and a molybdopterin-binding domain. The enzyme catalyzes the oxidation of sulfite to sulfate, the final reaction in the oxidative degradation of the sulfur amino acids cysteine and methionine. Sulfite oxidase deficiency results in neurological abnormalities which are often fatal at an early age. Alternative splicing results in multiple transcript variants encoding identical proteins.
References
Rajapakshe, A., et al. Biochemistry 49(25):5154-5159(2010)
Johnson-Winters, K., et al. Biochemistry 49(6):1290-1296(2010)
Neumann, M., et al. FEBS J. 275(22):5678-5689(2008)
Astashkin, A.V., et al. J. Am. Chem. Soc. 130(26):8471-8480(2008)
Hakonarson, H., et al. Diabetes 57(4):1143-1146(2008)
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