Analytical Data
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Gene name
NDUFB3
- Application
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Alternative Names
NDUFB3; NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3; Complex I-B12; CI-B12; NADH-ubiquinone oxidoreductase B12 subunit
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43676
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Expression Region
1-98 aa
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AA Sequence
MAHEHGHEHGHHKMELPDYRQWKIEGTPLETIQKKLAAKGLRDPWGRNEAWRYMGGFAKSVSFSDVFFKGFKWGFAAFVVAVGAEYYLESLNKDKKHH
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Molecular Weight
36.3 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
NDUFB3, a crucial component of the mitochondrial respiratory chain, is a subunit of complex I (NADH:ubiquinone oxidoreductase), which plays a pivotal role in cellular energy production through oxidative phosphorylation. Mutations in the NDUFB3 gene are associated with various mitochondrial disorders, leading to impaired energy metabolism and a range of clinical manifestations. Given the enzyme's essential function in ATP synthesis and its involvement in mitochondrial pathophysiology, research on NDUFB3 recombinant protein has garnered significant attention. Studies have focused on the characterization of its structure and function, understanding the molecular mechanisms underlying its role in electron transport, and investigating the effects of specific mutations on its activity. Additionally, recombinant NDUFB3 protein is increasingly utilized in the development of therapeutic strategies aimed at correcting mitochondrial dysfunction. By exploring the biochemical properties and interactions of NDUFB3 within the respiratory complex, researchers aim to uncover potential targets for intervention in mitochondrial diseases, thereby paving the way for novel treatments and enhancing our understanding of mitochondrial biology.
