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).
ETHE1 Polyclonal Antibody. Unconjugated. Raised in: Rabbit.
Liquid. 0.03% Proclin 300, 50% Glycerol, 0.01M PBS, PH 7.4.
>95%, Protein G purified
Recombinant Human Persulfide dioxygenase ETHE1, mitochondrial protein (8-254AA)
Shipped at 4°C. Upon delivery aliquot and store at -20°C (short-term) or -80°C (long-term). Avoid repeated freeze.
Persulfide dioxygenase ETHE1, mitochondrial (EC:22.214.171.124 Publications, ETHE1, HSCO, Ethylmalonic encephalopathy protein 1, Hepatoma subtracted clone one protein, Sulfur dioxygenase ETHE1
ELISA, WB, IHC; Recommended dilution: WB:1:500-2000, IHC:1:20-1:200