Analytical Data
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Gene name
AOX1
- Application
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Alternative Names
Aldehyde oxidase 1;Azaheterocycle hydroxylase (EC:1.17.3.-)
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Species
Human
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Source
E. coli
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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
Q06278
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Expression Region
236-421aa
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Molecular Weight
24.6 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
AOX1 (alcohol oxidase 1) is a key enzyme primarily found in methylotrophic yeasts, particularly in species such as *Pichia pastoris*. Its main function is to catalyze the oxidation of methanol to formaldehyde, which is an essential step in the assimilation of methanol as a carbon source. The study of AOX1 has gained significant interest due to its potential applications in biotechnology, particularly in recombinant protein production and metabolic engineering. In industrial settings, AOX1 is often utilized in expression systems to facilitate the production of heterologous proteins. Furthermore, the ability to manipulate the AOX1 promoter allows for controlled expression in response to methanol, enabling researchers to optimize yields. Advances in genetic engineering techniques have led to the exploration of AOX1's structure and function, revealing insights into its catalytic mechanism and substrate specificity. The ongoing research focuses on enhancing the efficiency of expression systems, understanding its role in methanol metabolism, and developing AOX1-based bioconversion systems for sustainable processes. By elucidating the properties and regulatory mechanisms of AOX1, scientists aim to leverage its capabilities for various biotechnological applications, contributing to the development of greener and more efficient production methods in the biosciences. As a model system, AOX1 continues to be a focal point in studies aimed at understanding enzyme kinetics, protein folding, and the intricacies of metabolic pathways.











