|Other Names||Persulfide dioxygenase ETHE1, mitochondrial, Ethylmalonic encephalopathy protein 1, Hepatoma subtracted clone one protein, Sulfur dioxygenase ETHE1, ETHE1, HSCO|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6641b was selected from the C-term region of human ETHE1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. First described as a protein that can shuttle between the nucleus and the cytoplasm and suppress p53-induced apoptosis by sequestering the transcription factor RELA/NFKB3 in the cytoplasm and preventing its accumulation in the nucleus (PubMed:12398897).|
|Cellular Location||Cytoplasm. Nucleus. Mitochondrion matrix|
|Tissue Location||Ubiquitously expressed.|
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Provided below are standard protocols that you may find useful for product applications.
ETHE1 is a sulfur dioxygenase that localizes within the mitochondrial matrix. The enzyme functions in sulfide catabolism. Mutations in its gene result in ethylmalonic encephalopathy.
Tiranti,V., Nat. Med. 15 (2), 200-205 (2009)Mineri,R., J. Med. Genet. 45 (7), 473-478 (2008)
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