Analytical Data
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Gene name
aroE
- Application
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Alternative Names
aroE; SERP1163; Shikimate dehydrogenase; NADP(+); SDH; EC 1.1.1.25
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Species
Staphylococcus epidermidis
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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
Q5HNV1
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Expression Region
1-269aa
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Molecular Weight
37.4 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
AroE recombinant protein research has gained significance in the fields of biotechnology and pharmaceuticals due to its potential applications in metabolic engineering and the synthesis of aromatic compounds. AroE, a gene encoding an enzyme involved in the shikimic acid pathway, plays a crucial role in the biosynthesis of aromatic amino acids and compounds, which are essential for various biological processes. The growing interest in renewable resources and sustainable production methods has led to the exploration of microbial systems that can efficiently produce these valuable compounds from inexpensive substrates. By harnessing AroE through recombinant DNA technology, researchers aim to enhance the metabolic capacity of host microorganisms, enabling them to convert simple carbon sources into high-value aromatic metabolites. This approach not only opens avenues for producing biofuels and other chemicals but also contributes to understanding the underlying biochemical mechanisms. Furthermore, with the increasing concerns regarding environmental pollution and reliance on fossil fuels, the development of sustainable processes utilizing AroE presents a promising solution for addressing global challenges. Studies on AroE recombinant protein can also provide insights into enzyme engineering and optimization, further improving yield and efficiency in industrial applications. Overall, the multifaceted relevance of AroE makes it an attractive target for research aimed at enhancing bioproduction and understanding metabolic pathways, positioning it at the forefront of contemporary biotechnological innovation.
