Recombinant Human ETHE1 protein (His tag N-Terminus)
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human ETHE1 protein (His tag N-Terminus) is a Human Full Length protein, in the 13 to 254 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
HSCO, ETHE1, Ethylmalonic encephalopathy protein 1, Hepatoma subtracted clone one protein, Sulfur dioxygenase ETHE1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human ETHE1 protein (His tag N-Terminus) (AB119454)
3ug by SDS-PAGE under reducing conditions and visualized by coomassie blue stain.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
ETHE1 assists in detoxifying potentially harmful sulfur compounds. It forms a part of a complex with sulfide:quinone oxidoreductase (SQR) and thiosulfate sulfurtransferase (TST) to facilitate efficient sulfur metabolism. The importance of ETHE1 lies in its ability to prevent the accumulation of toxic sulfide levels which can impair cellular respiration and energy production. The protein's role as a persulfide dioxygenase places it in a unique position as one of the body's defenses against sulfide toxicity.
Pathways
ETHE1 has significant relevance in the sulfide oxidation pathway and cellular respiration processes. Particularly it interacts with SQR in the mitochondrial matrix to convert hydrogen sulfide to thiosulfate and sulfite which then enter the citric acid cycle. This critical pathway is associated with energy production and efficient cellular function. The cooperation between ETHE1 and SQR ensures that toxic sulfide levels do not rise protecting mitochondrial integrity.
Specifications
Form
Liquid
General info
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).
Sequence similarities
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Subcellular localisation
Nucleus
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com