Analytical Data
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Gene name
atoD
- Application
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Alternative Names
Acetyl-CoA:acetoacetate-CoA transferase subunit alpha
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P76458
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Expression Region
1-220aa
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Molecular Weight
30.5 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
The study of the atoD recombinant protein arises from the increasing interest in understanding the metabolic pathways of bacteria, particularly those associated with the degradation of aromatic compounds. AtoD is a key component of the aromatic compound degradation pathway in certain bacteria, playing a crucial role in the conversion of aromatic intermediates into acetyl-CoA, a vital metabolic intermediate that feeds into various anabolic and catabolic processes. Given the environmental significance of these pathways, particularly in bioremediation efforts to detoxify pollutants, researchers have focused on characterizing the atoD gene and its protein product to enhance our understanding of microbial metabolic capabilities. The recombinant expression of AtoD allows for detailed studies of its enzymatic functions, protein structure, and interactions within metabolic networks. Additionally, insights gained from atoD research can potentially be applied to bioengineering efforts aimed at optimizing the bioconversion of lignocellulosic biomass into valuable biochemicals. By harnessing the functionalities of AtoD, scientists hope to develop more efficient biological systems for environmental cleanup and sustainable chemical production, addressing both ecological and industrial challenges.
