Analytical Data
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Gene name
NDUFB2
- Application
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Alternative Names
CI-AGGG; Complex I-AGGG; mitochondrial; NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2; NADH-ubiquinone oxidoreductase AGGG subunit; NDUB2_HUMAN; NDUFB2
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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
O95178
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Expression Region
34-105 aa
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AA Sequence
AGGGVHI EPRYRQFPQL TRSQVFQSEF FSGLMWFWIL WRFWHDSEEV LGHFPYPDPS QWTDEELGIP PDDED
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Molecular Weight
12.0 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
NDUFB2, a crucial subunit of the mitochondrial NADH:ubiquinone oxidoreductase (Complex I), plays a significant role in cellular energy metabolism within the oxidative phosphorylation pathway. This protein is integral to the electron transport chain, facilitating the transfer of electrons from NADH to ubiquinone, ultimately contributing to ATP production. Mutations in NDUFB2 have been linked to various mitochondrial diseases, which can result in severe cellular dysfunction and a wide array of clinical manifestations. The study of recombinant NDUFB2 protein is essential for understanding its structure and function, as well as its interactions with other Complex I components. By expressing and purifying this protein, researchers can elucidate the mechanistic pathways involved in mitochondrial bioenergetics, assess the impact of genetic variations, and develop potential therapeutic strategies for disorders associated with Complex I deficiencies. Furthermore, investigating the biochemical properties of recombinant NDUFB2 provides insights into the design of targeted interventions aimed at ameliorating mitochondrial dysfunction, highlighting its relevance in both basic and applied biomedical research.
