Analytical Data
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Gene name
NDUFB5
- Application
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Alternative Names
NDUFB5；NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5. mitochondrial
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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
O43674
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Expression Region
1-189aa
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AA Sequence
MAAMSLLRRVSVTAVAALSGRPLGTRLGFGGFLTRGFPKAAAPVRHSGDHGKRL FVIRPSRFYDRRFLKLLRFYIALTGIPVAIFITLVNVFIGQAELAEIPEGYVPE HWEYYKHPISRWIARNFYDSPEKIYERTMAVLQIEAEKAELRVKELEVRKLMHV RGDGPWYYYETIDKELIDHSPKATPDN
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Molecular Weight
31.7kDa
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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
Identification
Protein Description
NDUFB5, or NADH:ubiquinone oxidoreductase subunit B5, is a crucial component of the mitochondrial electron transport chain, specifically Part of Complex I. This protein plays a significant role in cellular energy production by facilitating the transfer of electrons from NADH to ubiquinone, a pivotal step in ATP synthesis. Research into NDUFB5 is particularly important due to its implications in various mitochondrial diseases and metabolic disorders. Mutations or deficiencies in this protein have been linked to impaired oxidative phosphorylation, leading to conditions such as Leigh syndrome and other severe neurological disorders. Additionally, NDUFB5 may have a role in regulating reactive oxygen species (ROS) production within mitochondria, further emphasizing its importance in cellular homeostasis. As mitochondrial dysfunction is a common feature in age-related diseases and conditions such as diabetes and neurodegenerative disorders, understanding NDUFB5's structure, function, and regulatory mechanisms can provide insights for potential therapeutic interventions. Consequently, recombinant studies of NDUFB5 are critical for elucidating its biochemical properties, interaction with other mitochondrial components, and developing strategies for gene therapy or enzyme replacement therapy aimed at restoring normal function in affected tissues. Overall, ongoing research into NDUFB5 holds promise for advancing our understanding of mitochondrial biology and addressing the challenges posed by related diseases.
