Analytical Data
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Gene name
toxA
- Application
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Alternative Names
tcdA
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Species
Clostridioides
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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
P16154
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Expression Region
2387-2710aa
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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
ToxA is a significant effector protein secreted by the plant pathogenic bacterium *Pseudomonas syringae*, which is known for its role in promoting plant diseases, especially in crops like tobacco. The study of ToxA has garnered interest due to its unique ability to induce specific symptoms in host plants, particularly the necrosis associated with the disease known as "tar spot." Research on recombinant forms of ToxA aims to elucidate its structure-function relationship and underlying mechanisms of action, facilitating a deeper understanding of plant-pathogen interactions. By producing recombinant ToxA in various expression systems, researchers can analyze its biochemical properties and assess its role in pathogenicity. Furthermore, characterizing ToxA can lead to the development of novel strategies for disease management, including the engineering of disease-resistant plant varieties or the design of targeted inhibitors that disrupt ToxA's function. As agricultural biosecurity becomes increasingly crucial in the face of climate change and globalization, investigating ToxA not only contributes to our basic knowledge of plant pathology but also holds potential for practical applications in sustainable agriculture and enhanced food security.
