Analytical Data
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Gene name
NDUFS5
- Application
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Alternative Names
NDUFS5;NADH dehydrogenase [ubiquinone] iron-sulfur Protein 5
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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
O43920
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Expression Region
1-106aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMPFLDIQKRFGLNIDRWLTIQSGEQPY KMAGRCHAFEKEWIECAHGIGYTRAEKECKIEYDDFVECLLRQKTMRRAG TIRKQRDKLIKEGKYTPPPHHIGKGEPRP
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Molecular Weight
15 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
NDUFS5, also known as NADH dehydrogenase (ubiquinone) Fe-S protein 5, is a crucial component of the mitochondrial respiratory chain, specifically part of complex I. This enzyme plays a pivotal role in cellular energy metabolism by facilitating the transfer of electrons from NADH to ubiquinone, thereby contributing to ATP production through oxidative phosphorylation. Mutations or deficiencies in NDUFS5 are associated with a spectrum of mitochondrial diseases that often manifest in neurological, muscular, and metabolic disorders. Researchers have been exploring NDUFS5 recombinant protein for its potential in understanding the enzymatic mechanisms of complex I dysfunction and for developing therapeutic strategies. By studying the structural and functional properties of NDUFS5, scientists aim to elucidate the pathophysiological effects of its defects and to identify biomarkers for disease diagnosis and progression. Additionally, the recombinant production of NDUFS5 enables high-throughput screening of small molecules that could serve as potential drug candidates, offering new avenues for the treatment of mitochondrial-related diseases. Overall, the study of NDUFS5 recombinant protein is not only vital for basic mitochondrial biology but also holds significant clinical implications in the development of targeted therapies for complex I-related disorders.
