Analytical Data
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Gene name
OXNAD1
- Application
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Alternative Names
Oxidoreductase NAD binding domain containing 1; Oxidoreductase NAD-binding domain-containing protein 1; Oxnad1; OXND1_HUMAN
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Species
Human
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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
Q96HP4
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Expression Region
18-312aa
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Molecular Weight
49.2 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
OXNAD1 is a relatively novel protein that has garnered attention in the field of molecular and cellular biology due to its potential role in cellular metabolism and oxidative stress response. As part of the NADH dehydrogenase family, OXNAD1 is believed to be involved in mitochondrial function and energy production, which are critical for maintaining cellular homeostasis. Research indicates that dysregulation of OXNAD1 may contribute to various diseases, including metabolic disorders and neurodegenerative conditions. The study of OXNAD1 recombinants offers insights into its structural and functional characteristics, facilitating the understanding of its biochemical pathways and interactions. High-level expression and purification of OXNAD1 in heterologous systems, such as bacteria or yeast, allow for detailed analyses of its enzymatic activity and regulatory mechanisms. Moreover, investigating the specific substrates and cofactors of OXNAD1 can shed light on its physiological roles and potential therapeutic applications. As researchers continue to explore the implications of OXNAD1 in health and disease, understanding this protein may open new avenues for developing targeted treatments that harness its functions to mitigate the effects of oxidative stress and improve metabolic health.
