Purity ~90% (SDS-PAGE). Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H2S) 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 H2S 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. Source: Recombinant protein corresponding to aa8-254 from human ETHE1, fused to His-SUMO-Tag at N-terminal, expressed in E. coli. Molecular Weight: ~43.1kD AA
Size
10ug, 50ug, 100ug
Concentration
n/a
Applications
n/a
Other Names
Ethylmalonic encephalopathy protein 1, Hepatoma subtracted clone one protein, Sulfur dioxygenase ETHE1