Analytical Data
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Gene name
iolO
- Application
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Alternative Names
Bifunctional nonphosphorylated sugar isomerase （D-erythrose/D-threose isomerase） （L-ribulose 3-epimerase） （R3E） （Nonphosphorylated sugar 3-epimerase） （Nonphosphorylated sugar aldose-ketose isomerase）
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Species
Thermotoga maritima
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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
Q9WYP7
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Expression Region
1-270aa
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Molecular Weight
37.9 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 research on the iolO (inositol catabolism operon) recombinant protein is driven by the increasing importance of understanding inositol's role in microbial metabolism and its potential applications in biotechnology and medicine. Inositol is a crucial sugar alcohol involved in various cellular processes, including cell signaling and osmoregulation. The iolO gene, part of the inositol operon, encodes a protein that facilitates the catabolism of inositol through its conversion into intermediates that can be utilized for energy and growth by certain microorganisms. Studies have shown that manipulating the expression of the iolO gene can enhance inositol metabolism, providing insights into microbial physiology and potential avenues for metabolic engineering. This is particularly relevant for industry applications where microbial systems are employed for biofuel production, bioremediation, and the synthesis of valuable bio-based products. Furthermore, exploring the structural and functional aspects of the iolO recombinant protein can lead to a better understanding of its enzymatic mechanisms and interactions within the cellular environment. This knowledge has the potential to inform the development of novel biocatalysts and therapeutic strategies, thereby contributing to the broader field of metabolic engineering and synthetic biology. As such, research on iolO recombinant protein not only expands our fundamental understanding of microbial metabolism but also opens up new possibilities for the application of microorganisms in sustainable technological development.
