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; Complex I-B9; CI-B9; NADH-ubiquinone oxidoreductase B9 subunit
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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
2-84 aa
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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
Related Products
Protein Description
NDUFA3 (NADH:ubiquinone oxidoreductase subunit A3) is a vital component of the mitochondrial complex I, which plays a crucial role in the cellular energy metabolism by facilitating the transfer of electrons from NADH to ubiquinone. Mutations or deficiencies in NDUFA3 have been linked to diverse mitochondrial disorders, resulting in a range of clinical manifestations, including neurological deficits and myopathies. Given its essential role in mitochondrial function, the study of NDUFA3 and its recombinant protein is significant for understanding the pathogenesis of related diseases and exploring potential therapeutic strategies. Recent advances in protein engineering techniques have enabled the successful expression and purification of recombinant NDUFA3, allowing for in-depth functional assays and structural studies. These investigations not only enhance our comprehension of the mechanistic roles of NDUFA3 in the electron transport chain but also provide insights into the regulation of mitochondrial bioenergetics. Furthermore, understanding the biochemical properties and interactions of recombinant NDUFA3 can pave the way for the development of targeted therapies aimed at correcting the defective mitochondrial functions associated with NDUFA3 mutations. Overall, the research on NDUFA3 recombinant protein is pivotal for unraveling the complexities of mitochondrial biology and addressing the challenges posed by mitochondrial diseases.
