Analytical Data
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Gene name
NDUFB1
- Application
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Alternative Names
Complex I-MNLL;CI-MNLL;NADH-ubiquinone oxidoreductase MNLL subunit
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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
O75438
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Expression Region
2-58 aa
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AA Sequence
VNLLQIVRDHWVHVLVPMGFVIGCYLDRKSDERLTAFRNKSMLFKRELQPSEEVTWK
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Molecular Weight
33.7 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
NDUFB1, a critical subunit of the mitochondrial respiratory chain complex I, plays an essential role in aerobic energy production via oxidative phosphorylation. Mutations or deficiencies in the NDUFB1 gene are linked to a range of neurodegenerative disorders, characterized by impaired ATP synthesis and increased reactive oxygen species (ROS) production. This has generated significant interest in studying NDUFB1 to better understand mitochondrial dysfunction in various diseases. The recombinant protein of NDUFB1 can be produced in model organisms or expression systems, facilitating investigations into its structure, function, and interactions within the mitochondrial complex. By elucidating the biochemical properties and regulatory mechanisms of NDUFB1, researchers aim to uncover potential therapeutic targets and strategies for combating mitochondrial diseases. Additionally, advanced techniques such as cryo-electron microscopy and mass spectrometry are being employed to study the protein's conformation and dynamics in response to cellular stress. Overall, the research surrounding NDUFB1 recombinant protein not only enhances our understanding of mitochondrial bioenergetics but also provides insights into the molecular underpinnings of metabolic diseases, potentially guiding the development of novel interventions.
