protein

ETHE1 Protein, Human (His)

HY-P76324

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

52;88;247;420;1100;1800 USD

ETHE1 Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

52;88;247;420;1100;1800 USD

The ETHE1 protein is an important sulfur dioxygenase that plays an integral role in mitochondrial hydrogen sulfide catabolism.It cooperates with SQRDL to oxidize cysteine persulfide residues formed from hydrogen sulfide (H2S), preventing the accumulation of toxic H2S and maintaining metabolic homeostasis.ETHE1 Protein, Human (His) is the recombinant human-derived ETHE1 protein, expressed by E.coli , with N-His labeled tag.

Human

ETHE1 protein serves as a crucial sulfur dioxygenase playing an indispensable role in hydrogen sulfide catabolism within the mitochondrial matrix. In this process, hydrogen sulfide (H(2)S) is initially oxidized by SQRDL, forming cysteine persulfide residues. ETHE1, utilizing molecular oxygen, catalyzes the subsequent oxidation of the persulfide once it has been transferred to a thiophilic acceptor like glutathione (R-SSH). This enzymatic activity is vital for maintaining metabolic homeostasis in mitochondria, preventing the accumulation of supraphysiological H(2)S levels that could be toxic due to the inhibition of cytochrome c oxidase. Beyond its role in hydrogen sulfide metabolism, ETHE1 was initially identified as a protein capable of shuttling between the nucleus and the cytoplasm. It suppresses p53-induced apoptosis by sequestering the transcription factor RELA/NFKB3 in the cytoplasm, preventing its accumulation in the nucleus.

Persulfide dioxygenase ETHE1; Sulfur dioxygenase ETHE1; HSCO

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.