Analytical Data
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Gene name
NDUFB11
- Application
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Alternative Names
NDUFB11; UNQ111/PRO1064; NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11. mitochondrial; Complex I-ESSS; CI-ESSS; NADH-ubiquinone oxidoreductase ESSS subunit; Neuronal protein 17.3; Np17.3; p17.3
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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
Q9NX14
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Expression Region
1-153 aa
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AA Sequence
MAAGLFGLSARRLLAAAATRGLPAARVRWESSFSRTVVAPSAVAGKRPPEPTTPWQEDPEPEDENLYEKNPDSHGYDKDPVLDVWNMRLVFFFGVSIILVLGSTFVAYLPDYRMKEWSRREAERLVKYREANGLPIMESNCFDPSKIQLPEDE
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Molecular Weight
42.57 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
NDUFB11, a subunit of the mitochondrial NADH:ubiquinone oxidoreductase (complex I), plays a critical role in aerobic respiration and ATP production within the mitochondria. Dysfunctions in this protein have been implicated in various mitochondrial diseases, particularly those related to energy metabolism. Research has increasingly focused on NDUFB11 due to its potential link to neurodegenerative disorders, including Parkinson's disease and other conditions associated with mitochondrial dysfunction. The study of recombinant NDUFB11 proteins offers a unique opportunity to elucidate their structure-function relationships and to explore the biochemical pathways they participate in. By generating and characterizing recombinant NDUFB11, researchers aim to understand the molecular mechanisms underlying its role in energy production and to identify potential therapeutic targets for treating mitochondrial diseases. Moreover, recombinant NDUFB11 can be utilized in functional assays and structural studies, providing insights into the interactions with other subunits of complex I and elucidating how mutations may disrupt normal function. This research holds promise not only for advancing our understanding of mitochondrial biology but also for developing new strategies to combat diseases stemming from mitochondrial dysfunction.
