Analytical Data
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Gene name
NDUFB10
- Application
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Alternative Names
Complex I-PDSW
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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
O96000
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Expression Region
1-172aa
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Molecular Weight
47.8 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
NDUFB10, a nuclear-encoded subunit of the mitochondrial NADH:ubiquinone oxidoreductase complex (Complex I), plays a crucial role in cellular energy metabolism. This protein is integral to the electron transport chain, facilitating the transfer of electrons from NADH to ubiquinone, ultimately supporting ATP production through oxidative phosphorylation. Mutations in the NDUFB10 gene have been linked to various mitochondrial diseases, characterized by impaired energy production and associated with symptoms such as muscle weakness, neurological deficits, and metabolic dysfunction. The study of NDUFB10 recombinant protein is significant for understanding the molecular mechanisms underlying these mitochondrial disorders. By expressing and purifying recombinant NDUFB10, researchers aim to investigate its structure, function, and interaction with other Complex I components, thereby gaining insights into its role in mitochondrial bioenergetics. Furthermore, developing a reliable supply of this protein opens avenues for potential therapeutic strategies aimed at correcting the functional deficits caused by NDUFB10 mutations. Ultimately, advancing our understanding of NDUFB10's biochemical properties and its contributions to mitochondrial function may lead to improved diagnostic tools and targeted treatments for mitochondrial diseases.
