Analytical Data
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Gene name
NDUFS6
- Application
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Alternative Names
NDUFS6;NADH dehydrogenase [ubiquinone] iron-sulfur Protein 6. 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
O75380
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Expression Region
28-124aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSFGVRVSP TGEKVTHTGQ VYDDKDYRRI RFVGRQKEVN ENFAIDLIAE QPVSEVETRV IACDGGGGAL GHPKVYINLD KETKTGTCGY CGLQFRQHHH
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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
NDUFS6 is an essential protein component of the mitochondrial respiratory chain complex I, playing a critical role in cellular energy metabolism. Deficiencies in NDUFS6 have been linked to a range of mitochondrial disorders, resulting in impaired ATP production and various clinical manifestations including neurological deficits, myopathy, and cardiomyopathy. The study of NDUFS6 is significant not only for understanding the molecular mechanisms underlying mitochondrial diseases but also for exploring potential therapeutic strategies. Recent advances in recombinant protein technology have enabled researchers to produce NDUFS6 in vitro, facilitating functional studies and investigations into its interactions with other complex I subunits. These studies aim to unravel the structural and functional dynamics of complex I and its assembly processes. Moreover, understanding the pathophysiological effects of NDUFS6 mutations could lead to the development of targeted gene therapies or pharmacological interventions to ameliorate symptoms in affected individuals. As mitochondrial dysfunction is a contributing factor in numerous age-related diseases, research on NDUFS6 could also provide insights into broader aspects of mitochondrial biology and its implications for aging and metabolic health. Overall, the investigation of NDUFS6 and its recombinant forms holds promise for both basic research and the development of novel therapeutic approaches in mitochondrial disease.
