Analytical Data
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Gene name
NDUFA12
- Application
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Alternative Names
13KDA differentiation-associated protein Complex I-B17.2
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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
Q9UI09
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Expression Region
1-145aa
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Molecular Weight
44.1 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
NDUFA12, a gene encoding a subunit of the mitochondrial respiratory chain complex I (NADH:ubiquinone oxidoreductase), plays a crucial role in oxidative phosphorylation, a fundamental process for ATP production in eukaryotic cells. The study of NDUFA12 recombinant protein is significant due to its implications in mitochondrial function and energy metabolism. Deficiencies or mutations in NDUFA12 have been linked to various mitochondrial diseases, leading to metabolic dysfunction and neurodegenerative disorders. By expressing and characterizing recombinant NDUFA12, researchers aim to gain deeper insights into its structural and functional properties, elucidating its role in complex I assembly and stability. Furthermore, understanding the biochemical pathways involving NDUFA12 can contribute to developing therapeutic strategies for mitochondrial diseases. Recent advances in recombinant protein technology and structural biology allow for detailed studies, enabling the exploration of NDUFA12 interactions with other subunits and cofactors involved in mitochondrial respiration. Such research not only furthers our understanding of mitochondrial bioenergetics but also highlights the potential for targeted interventions in mitochondrial dysfunction-related diseases.
