Analytical Data
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Gene name
trhO
- Application
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Alternative Names
(34)(tRNA hydroxylation protein O)
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Species
Chlamydia felis
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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
Q252M0
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Expression Region
1-325aa
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Molecular Weight
43.6 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
TrhO protein, an essential component in the study of microbial metabolic processes, has garnered significant attention due to its role in the regulation of metabolic pathways in various organisms. Initially identified in certain bacteria, TrhO is implicated in the synthesis and degradation of small molecules critical for cellular function and growth. Research has demonstrated that TrhO is involved in the catabolism of specific substrates, such as amino acids and carbohydrates, which are vital for energy production and cellular maintenance. Furthermore, the protein's unique structural features, including its binding sites and enzymatic activities, provide insights into its functionality and potential applications in biotechnology and synthetic biology. Scientists are keen to explore the therapeutic potential of TrhO in addressing metabolic disorders and its utility in engineering microbial strains for enhanced production of biofuels and biochemicals. As the understanding of TrhO continues to evolve, its significance in metabolic engineering and environmental sustainability is becoming increasingly evident, positioning it as a target for innovative research and development endeavors.
