Analytical Data
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Gene name
NDUFB8
- Application
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Alternative Names
NDUFB8; NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8. mitochondrial; Complex I-ASHI; CI-ASHI; NADH-ubiquinone oxidoreductase ASHI 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
O95169
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Expression Region
1-186 aa
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AA Sequence
MAVARAGVLGVQWLQRASRNVMPLGARTASHMTKDMFPGPYPRTPEERAAAAKKYNMRVEDYEPYPDDGMGYGDYPKLPDRSQHERDPWYSWDQPGLRLNWGEPMHWHLDMYNRNRVDTSPTPVSWHVMCMQLFGFLAFMIFMCWVGDVYPVYQPVGPKQYPYNNLYLERGGDPSKEPERVVHYEI
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Molecular Weight
46.2 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
NDUFB8, a subunit of the mitochondrial complex I, plays a crucial role in the electron transport chain, facilitating ATP production through oxidative phosphorylation. Research into NDUFB8 has gained prominence due to its implications in various mitochondrial disorders and its association with neurodegenerative diseases, such as Parkinson's disease. Mutations or deficiencies in NDUFB8 can lead to impaired mitochondrial function, resulting in decreased energy production and increased oxidative stress, contributing to cellular dysfunction. Given the importance of NDUFB8 in energy metabolism and disease pathology, scientists are increasingly focused on understanding its structure, function, and the mechanisms by which it influences mitochondrial health. Recombinant NDUFB8 proteins are being produced to study their biochemical properties, interactions with other mitochondrial components, and potential therapeutic applications. The investigation into NDUFB8 not only enhances our understanding of mitochondrial biology but also paves the way for developing targeted therapies for conditions linked to mitochondrial dysfunction. Overall, the research surrounding NDUFB8 and its recombinant forms holds significant promise for advancing our knowledge of mitochondrial diseases and improving therapeutic strategies.
