Analytical Data
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Gene name
pntA
- Application
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Alternative Names
Nicotinamide nucleotide transhydrogenase subunit alphaPyridine nucleotide transhydrogenase subunit alpha
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Species
Escherichia coli
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P07001
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Expression Region
1-401aa
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Molecular Weight
44.8 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
Related Products
Protein Description
The study of the pntA recombinant protein is rooted in its essential role in cellular metabolism and energy production in various organisms. pntA encodes a component of the pyridine nucleotide transhydrogenase complex, which is critical for the interconversion of NADH and NADPH, two key coenzymes involved in redox reactions. This protein facilitates the maintenance of cellular redox balance, playing a vital role in processes such as respiration, photosynthesis, and biosynthetic pathways. Recent advances in molecular cloning and protein expression techniques have enabled the production of pntA recombinant protein, allowing researchers to investigate its biochemical properties and functional mechanisms in greater detail. Understanding the structure and function of pntA not only provides insights into fundamental metabolic pathways but also holds potential implications for biotechnological applications, such as optimizing microbial fermentation processes or developing novel metabolic engineering strategies. Additionally, the study of pntA and its associated complexes can reveal evolutionary adaptations in various organisms, shedding light on how different species have developed unique strategies for energy conservation and efficiency. Overall, research on pntA recombinant protein presents a valuable opportunity to explore its contributions to metabolic regulation and its potential applications in biotechnology and synthetic biology.
