Analytical Data
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Gene name
NDUFA3
- Application
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Alternative Names
NDUFA3；NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
AARVGAFLKNAWDKEPVLVVSFVVGGLAVILPPLSPYFKYSVMINKATPYNYPVPVRDDGNMPDVPSHPQDPQGPSLEWLKKL
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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 nuclear-encoded protein that is part of the mitochondrial respiratory chain complex I (NADH:ubiquinone oxidoreductase), plays a pivotal role in cellular energy metabolism. This protein is essential for efficient mitochondrial function, as it contributes to the transfer of electrons from NADH to ubiquinone, facilitating ATP production through oxidative phosphorylation. Dysregulation or mutations in the NDUFA3 gene have been linked to various mitochondrial diseases and metabolic disorders, underscoring its importance in human health. Researchers are increasingly focused on the structural and functional characterization of NDUFA3, aiming to understand its precise role in complex I assembly and activity. Additionally, the potential application of NDUFA3 as a biomarker for mitochondrial dysfunction has sparked interest in its therapeutic implications. Recombinant NDUFA3 proteins are being studied to investigate their interactions with other respiratory chain components, evaluate their enzymatic activity, and explore their potentials in restoring mitochondrial function in affected conditions. Through these investigations, insights into the pathophysiology of mitochondrial diseases may be gained, paving the way for novel therapeutic strategies targeting NDUFA3-related dysfunctions in energy metabolism.
