Analytical Data
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Gene name
NDUFB7
- Application
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Alternative Names
Cell adhesion protein SQM1Complex I-B18 ;CI-B18NADH-ubiquinone oxidoreductase B18 subunit
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17568
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Expression Region
2-137aa
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Molecular Weight
43.3 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
Related Products
Protein Description
NDUFB7, a crucial component of the mitochondrial respiratory chain, plays an essential role in the function of complex I, which is responsible for the NADH:ubiquinone oxidoreductase activity. This enzyme complex is fundamental for ATP production through oxidative phosphorylation, making it vital for cellular energy metabolism. Research has shown that mutations in the NDUFB7 gene can lead to severe mitochondrial diseases, resulting in a range of clinical manifestations including neurological disorders, muscle weakness, and organ dysfunction. Understanding the structure and function of NDUFB7 is therefore critical for elucidating the mechanisms of mitochondrial dysfunction and developing potential therapeutic interventions. Recombinant NDUFB7 proteins are increasingly used in biochemical and structural studies to investigate their interactions with other mitochondrial components, the effects of pathological mutations, and the overall assembly of complex I. By generating and characterizing these recombinant proteins, researchers aim to provide insights into the intricacies of mitochondrial energy metabolism, paving the way for advancements in treating related disorders. The ongoing study of NDUFB7 also highlights the importance of mitochondrial health in aging and various metabolic conditions, emphasizing the need for continued exploration of this protein's role in mitochondrial biology.
