Analytical Data
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Gene name
ETHE1
- Application
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Alternative Names
Ethylmalonic encephalopathy protein 1Hepatoma subtracted clone one protein;Sulfur dioxygenase ETHE1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95571
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Expression Region
8-254aa
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Molecular Weight
43.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ETHE1 is a protein associated with the human mitochondrial sulfur metabolic pathway, playing a crucial role in maintaining cellular redox homeostasis. Mutations in the ETHE1 gene have been linked to a rare autosomal recessive disorder known as ethylmalonic encephalopathy, which is characterized by neurological dysfunction, short stature, and metabolic abnormalities. Research into ETHE1 has gained significance due to its involvement in hydrogen sulfide metabolism and mitochondrial function, which are essential for energy production and detoxification processes within cells. Recent studies have focused on understanding the structural and functional properties of the ETHE1 protein, revealing insights into its enzymatic mechanisms and interactions with other cellular components. This research is vital not only for elucidating the pathophysiology of related disorders but also for developing potential therapeutic strategies aimed at alleviating symptoms associated with ETHE1 dysfunction. By investigating the dynamics of ETHE1, scientists aim to enhance our comprehension of mitochondrial diseases and contribute to the broader field of metabolic research, potentially leading to novel interventions for patients suffering from mitochondrial disorders.
