Analytical Data
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Gene name
aexT
- Application
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Alternative Names
aexT；ADP-ribosyltransferase toxin AexT
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q93Q17
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Expression Region
1-475aa
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AA Sequence
MQIQANTVGTQAVAHHSDATTGVGRMGQMEARQVATGQDAILLGSRSEPQKGQGLLSRLGAQLARPFVAIKEWISNLLGTDKRAAAPKAQTAVSPEDLQRLMKQAAFGSSLGGFAKADVLNNITGEQLGKDHASLATGNGPLRSLCTALQAVVIGSQQPQLRELATGLLARPIAGIPLQQWGSVGGKVTELLTSAPPELLKEAMSQLHTAMGEVADLQRAVKAEVAGEPARSATTAAAVAPLQSGESEVNVEPADKALAEGLQEQFGLEAEQYLGEQPHGTYSDAEVMALGLYTNGEYQHLNRSLRQEKQLDAGQALIDQGMSTAFEKSTPTEQLIKTFRGTHGGDAFNEVAEGQVGHDVAYLSTSRDPKVATNFGGSGSISTIFGRSGIDVSDISVEGDEQEILYNKETDMRVLLSAKDERGVTRRVLEEASLGEQSGHSKGLLDGLDLARGAGGADKPQEQDIRLKMRGLDLA
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Molecular Weight
66.1 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
Related Products
Protein Description
AexT, a protein derived from the biocontrol fungus *Aspergillus flavus*, has garnered significant interest in research due to its potential applications in agriculture and biotechnology. As a pathogenic strain, *A. flavus* is notorious for producing aflatoxins, which are highly toxic and carcinogenic, posing substantial risks to food safety and human health. However, AexT exhibits unique biocontrol properties that enable it to inhibit the growth of various plant pathogens, thereby promoting plant health and enhancing crop yields. Understanding the molecular mechanisms underlying AexT's activity is crucial for leveraging its potential in agricultural practices. Recent advances in protein engineering and characterization techniques have facilitated in-depth studies of AexT's structure and function, paving the way for the development of novel biopesticides and environmentally friendly agricultural solutions. Researchers aim to explore AexT’s interactions with target plant pathogens and elucidate its efficacy in diverse agricultural settings, seeking to provide sustainable alternatives to chemical pesticides. Through these investigations, AexT can be positioned as a vital component in integrated pest management strategies, contributing to more resilient and sustainable agricultural ecosystems.
