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.

Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.

254 amino acids

MAGSVLKIAGRRLSQHTGSGAPVLLRQMFEPKSCTYTYLLGDRESREAVLIDPVLETAQRDAQLVKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRLSGAQADWHIEDGDSIQFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAETLYHSVHEKIFTLPGNCLIYPAHDYHGLTVSTVEEERTLNPRLTLSCEEFVKVMDKLNLPKPQQIDFAVPANMRCGIQTPPS

27.9 kDa

(Note: Representative image - actual molecular weight may vary depending on tag type and expression method)

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