Analytical Data
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Gene name
NDUFAF3
- Application
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Alternative Names
3orf60; NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 3; NDUF3_HUMAN; ndufaf3
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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
Q9BU61
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Expression Region
1-184 aa
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AA Sequence
MATALALRSL YRARPSLRCP PVELPWAPRR GHRLSPADDE LYQRTRISLL QREAAQAMYI DSYNSRGFMI NGNRVLGPCA LLPHSVVQWN VGSHQDITED SFSLFWLLEP RIEIVVVGTG DRTERLQSQV LQAMRQRGIA VEVQDTPNAC ATFNFLCHEG RVTGAALIPP PGGTSLTSLG QAAQ
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Molecular Weight
20.3 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
NDUFAF3, a pivotal protein involved in mitochondrial function, plays a critical role in the assembly and stability of the NADH: ubiquinone oxidoreductase complex (Complex I) within the mitochondrial respiratory chain. Dysfunction in Complex I is implicated in various mitochondrial diseases and neurodegenerative disorders, highlighting the importance of NDUFAF3 in cellular energy metabolism. Research has shown that NDUFAF3 is essential for the incorporation of specific mitochondrial-encoded subunits into Complex I, and its absence can lead to reduced enzyme activity and impaired mitochondrial respiration. Given its significant role in maintaining mitochondrial integrity and function, NDUFAF3 has garnered attention in studies aiming to understand the molecular mechanisms underlying mitochondrial pathologies. Furthermore, understanding its structure and function could provide insights into therapeutic interventions for Complex I-related diseases. Recent advancements in recombinant protein technology have allowed for the production and analysis of NDUFAF3, paving the way for further studies elucidating its interactions with other mitochondrial proteins and its contribution to respiratory chain assembly. This research is crucial for developing potential strategies to mitigate mitochondrial dysfunction and improve outcomes in related disorders.
