Analytical Data
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Gene name
tadA
- Application
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Species
Escherichia coli O157:H7
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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
Q8XA44
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Expression Region
1-167aa
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Molecular Weight
22.8 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
tadA, or tRNA adenosine deaminase, is an essential enzyme involved in the post-transcriptional modification of tRNA molecules, specifically catalyzing the hydrolytic deamination of adenosine to inosine at the wobble position of tRNA. This modification plays a critical role in enhancing codon recognition during protein synthesis, thereby influencing the efficiency and accuracy of translation. The research on tadA recombinant proteins has gained momentum due to its potential applications in biotechnology, including the development of novel therapeutic strategies and gene editing technologies like CRISPR-Cas9. Understanding the structure-function relationship of tadA can provide insights into its enzymatic mechanism and regulation. Furthermore, studying recombinant tadA proteins can facilitate improvements in the stability and activity of this enzyme for use in various applications, such as the engineering of tRNA for enhanced expression of proteins in heterologous systems. Advances in expression systems and purification techniques for tadA recombinants have opened new avenues for investigating its role in cellular metabolism, as well as its implications in diseases linked to tRNA modifications. Overall, the study of tadA and its recombinant forms is crucial for both fundamental biochemical research and practical applications in synthetic biology and medicine.
