Analytical Data
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Gene name
NDUFA3
- Application
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Alternative Names
Complex I-B9 ;CI-B9NADH-ubiquinone oxidoreductase B9 subunit
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95167
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Expression Region
2-84aa
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Molecular Weight
36.1 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
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Protein Description
NDUFA3, a critical subunit of the mitochondrial respiratory chain complex I, plays a vital role in cellular energy metabolism. This protein is essential for the assembly and stability of complex I, which is responsible for the critical task of oxidative phosphorylation in eukaryotic cells. Dysfunction or mutations in NDUFA3 have been implicated in various mitochondrial diseases and disorders, including neurodegenerative conditions and metabolic syndromes. Research on NDUFA3 recombinant protein has gained attention as it allows for the exploration of its structural and functional properties, facilitating our understanding of the biochemical pathways involved in ATP production. By producing NDUFA3 in a recombinant form, scientists can investigate the effects of specific mutations, delineate the protein's interactions within the electron transport chain, and evaluate potential therapeutic interventions for associated mitochondrial dysfunctions. Furthermore, studies of NDUFA3 could provide insights into broader mitochondrial biology, including signaling pathways related to apoptosis, oxidative stress, and cellular response to energy demands. Understanding NDUFA3 at the molecular level not only sheds light on fundamental biological processes but also holds promise for developing strategies to combat diseases associated with mitochondrial dysfunctions. Hence, research focusing on the recombinant expression and characterization of NDUFA3 is crucial for advancing our comprehension of mitochondrial biology and its implications for human health.
