Analytical Data
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Gene name
NDUFB6
- Application
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Alternative Names
NDUFB6; NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6; Complex I-B17; CI-B17; NADH-ubiquinone oxidoreductase B17 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
O95139
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Expression Region
1-128 aa
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AA Sequence
MTGYTPDEKLRLQQLRELRRRWLKDQELSPREPVLPPQKMGPMEKFWNKFLENKSPWRKMVHGVYKKSIFVFTHVLVPVWIIHYYMKYHVSEKPYGIVEKKSRIFPGDTILETGEVIPPMKEFPDQHH
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Molecular Weight
39.82 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
NDUFB6, a subunit of the mitochondrial NADH-ubiquinone oxidoreductase (Complex I), plays a critical role in the mitochondrial electron transport chain, facilitating the conversion of NADH into ubiquinone while contributing to the generation of a proton gradient necessary for ATP synthesis. Mutations and dysfunctions in NDUFB6 have been implicated in various mitochondrial disorders, leading to a spectrum of pathologies, including neurodegenerative diseases and myopathies. The study of recombinant NDUFB6 protein is important for understanding its structural and functional properties, as well as its interactions within the larger Complex I assembly. Researchers aim to elucidate the mechanistic details of its role in electron transfer and its potential involvement in the regulation of oxidative phosphorylation. By producing recombinant NDUFB6, scientists can perform biochemical assays, investigate its interactions with other complex I subunits, and assess the impact of specific mutations. This research not only contributes to our understanding of mitochondrial biology but also has implications for the development of therapeutic strategies targeting mitochondrial dysfunction. Thus, the study of NDUFB6 at a molecular level is paramount for unraveling the complexities of cellular energy metabolism and addressing mitochondrial-related diseases.
