Analytical Data
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Gene name
aexT
- Application
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Alternative Names
Exoenzyme T
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Species
Aeromonas salmonicida
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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
Q93Q17
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Expression Region
1-475aa
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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
The study of aexT recombinant proteins is rooted in the broader field of molecular biology and biotechnology, where understanding protein function and interaction is crucial for various applications, including drug development and therapeutic interventions. aexT, a gene derived from certain bacterial species, encodes a protein that has shown potential in various biological processes, including virulence factors and immune response modulation. Research into aexT recombinant proteins aims to harness their properties for developing novel biomolecules with enhanced functionalities. The ability to produce these proteins in recombinant systems allows for detailed characterization and optimization of their biochemical properties. Furthermore, aexT's role in pathogen-host interactions makes it a candidate for further investigation into the mechanisms of infection and immunity, which could lead to novel vaccines or therapeutics. As the demand for precise and effective biotherapeutics grows, studying aexT and its recombinant counterparts could provide critical insights into microbial physiology and therapeutic targets, ultimately contributing to improved healthcare solutions.
