Analytical Data
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Gene name
MT-ND1
- Application
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Alternative Names
NADH dehydrogenase subunit 1 MTND1, NADH1, ND1
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Species
Lampetra fluviatilis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O21069
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Expression Region
1-321aa
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Molecular Weight
53.8 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
MT-ND1, a subunit of mitochondrial complex I, is crucial for cellular respiration and energy production. It plays a vital role in the electron transport chain, contributing to ATP synthesis. Mutations in the MT-ND1 gene are implicated in various mitochondrial disorders, which can lead to neurodegenerative diseases, muscle weakness, and developmental issues. Given these significant associations, understanding the structure and function of MT-ND1 is essential for elucidating the pathophysiology of mitochondrial diseases. Researchers focus on characterizing its protein structure through methods like X-ray crystallography and cryo-electron microscopy, which can reveal insights into its interactions with other complex I subunits. This knowledge may lead to the development of targeted therapies aimed at mitigating the effects of MT-ND1-related mitochondrial dysfunction. The exploration of MT-ND1 recombinant proteins also provides a platform for investigating its biochemical properties, interactions, and potential as a therapeutic target. In summary, the study of MT-ND1 recombinant protein is critical for advancing our understanding of mitochondrial bioenergetics and developing innovative strategies to address mitochondrial diseases.
