Analytical Data
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Gene name
AEN
- Application
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Alternative Names
Interferon-stimulated 20KDA exonuclease-like 1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WTP8
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Expression Region
117-325aa
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Molecular Weight
40.1 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
AEN (Aminoacyl-tRNA Editing Nuclease) is a crucial protein associated with the fidelity of protein synthesis in cells, specifically in the context of tRNA editing. The research surrounding AEN has gained traction due to its pivotal role in preventing errors during aminoacylation, where tRNA molecules are charged with their corresponding amino acids. Misacylation can lead to the incorporation of incorrect amino acids into proteins, resulting in malfunctioning enzymes and altered cellular functions. The study of AEN is particularly relevant as it offers insights into the mechanisms of translation accuracy and its implications in various diseases, including cancer and genetic disorders. Recent advances have elucidated the structure-function relationships of AEN, revealing its catalytic properties and interactions with tRNA substrates. These findings pave the way for potential therapeutic applications, such as developing drugs that target the AEN pathway to enhance or inhibit its function, thereby providing a novel approach to rectify translation errors that contribute to disease pathology. Understanding the recombinant expression of AEN and the characterization of its activity can also facilitate the development of biotechnological applications, including the engineering of more accurate protein synthesis systems. Overall, the ongoing research into AEN is crucial not only for fundamental biology but also for its potential applications in medicine and biotechnology.











