Analytical Data
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Gene name
NDUFA11
- Application
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Alternative Names
NDUFA11; NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11; Complex I-B14.7; CI-B14.7; NADH-ubiquinone oxidoreductase subunit B14.7
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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
Q86Y39
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Expression Region
1-141 aa
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AA Sequence
MAPKVFRQYWDIPDGTDCHRKAYSTTSIASVAGLTAAAYRVTLNPPGTFLEGVAKVGQYTFTAAAVGAVFGLTTCISAHVREKPDDPLNYFLGGCAGGLTLGARTHNYGIGAAACVYFGIAASLVKMGRLEGWEVFAKPKV
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Molecular Weight
41.3 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
NDUFA11, a crucial component of the mitochondrial respiratory chain, plays a significant role in cellular energy metabolism. It is part of the NADH:ubiquinone oxidoreductase (complex I), which is essential for ATP production through oxidative phosphorylation. Mutations or dysfunctions in NDUFA11 have been linked to various mitochondrial disorders and can lead to severe neurological and muscular diseases due to impaired energy production. Research on the recombinant NDUFA11 protein has gained momentum as scientists aim to understand its structure-function relationships, enzymatic activity, and interaction with other complexes in the electron transport chain. The expression of recombinant NDUFA11 allows for the study of its biochemical properties and the effects of specific mutations, facilitating insights into disease mechanisms. This research not only enhances our understanding of mitochondrial pathophysiology but also opens potential avenues for therapeutic interventions targeting mitochondrial dysfunctions. Additionally, the production of recombinant NDUFA11 may aid in the development of drug screening assays and help identify compounds that can restore the functionality of complex I in affected individuals. Overall, the investigation of NDUFA11 through recombinant protein studies is a vital step toward unraveling the complexities of mitochondrial biology and developing strategies to treat related disorders.
