Analytical Data
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Gene name
NDUFB10
- Application
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Alternative Names
NDUFB10；NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
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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
O96000
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Expression Region
1-172aa
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AA Sequence
MPDSWDKDVYPEPPRRTPVQPNPIVYMMKAFDLIVDRPVTLVREFIERQHAKNRYYYYHRQYRRVPDITECKEEDIMCMYEAEMQWKRDYKVDQEIINIMQDRLKACQQREGQNYQQNCIKEVEQFTQVAKAYQDRYQDLGAYSSARKCLAKQRQRMLQERKAAKEAAAATS
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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
Related Products
Protein Description
NDUFB10, a subunit of the mitochondrial respiratory chain complex I (NADH:ubiquinone oxidoreductase), plays a crucial role in cellular energy metabolism by facilitating electron transfer and proton translocation across the mitochondrial membrane. Abnormalities in NDUFB10 function can lead to various mitochondrial diseases, which are often characterized by energy deficiency and impaired oxidative phosphorylation. The investigation of NDUFB10 recombinant proteins has gained significant attention in recent years, as understanding its structure and function is essential for elucidating the molecular mechanisms underlying complex I-related pathologies. Studies have shown that mutations in the NDUFB10 gene are linked to severe mitochondrial dysfunction, highlighting the importance of this protein in maintaining mitochondrial integrity and function. Furthermore, recombinant NDUFB10 proteins offer a valuable tool for assessing the impact of specific mutations on complex I activity and exploring potential therapeutic strategies. By characterizing the biophysical properties and biochemical interactions of NDUFB10, researchers aim to develop targeted interventions that could ameliorate mitochondrial disorders, thereby improving the quality of life for affected individuals. Overall, the comprehensive study of NDUFB10 recombinant proteins promises to enhance our understanding of mitochondrial bioenergetics and pave the way for innovative therapeutic approaches in mitochondrial medicine.
