Analytical Data
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Gene name
NDUFB4
- Application
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Alternative Names
NDUFB4;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
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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
O95168
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Expression Region
1-87aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSFPKYK PSSLRTLPET LDPAEYNISP ETRRAQAERL AIRAQLKREY LLQYNDPNRR GLIENPALLR WAYARTINVY PNFRPTPKNS
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Molecular Weight
13 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
NDUFB4, a crucial subunit of the mitochondrial respiratory chain complex I, plays a significant role in cellular energy metabolism. Located in the inner mitochondrial membrane, it is involved in the transfer of electrons from NADH to ubiquinone, a fundamental step in oxidative phosphorylation. Research into NDUFB4 has gained traction due to its implications in various metabolic disorders and neurodegenerative diseases, where mitochondrial dysfunction is often a hallmark. Studies have shown that mutations or alterations in the expression of NDUFB4 can lead to impaired mitochondrial function, contributing to conditions such as Leigh syndrome and other complex I deficiencies. The generation of recombinant NDUFB4 protein has opened avenues for in-depth investigations into its structural and functional characteristics, facilitating the understanding of its role in the respiratory chain. Additionally, the study of NDUFB4 is crucial for developing potential therapeutic strategies aimed at restoring mitochondrial function in affected individuals. Given its importance in bioenergetics and disease, ongoing research focuses on elucidating the mechanisms by which NDUFB4 operates within the complex I assembly and the broader implications of its dysregulation in human health.
