Analytical Data
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Gene name
toxA
- Application
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Alternative Names
toxA；Polymeric immunoglobulin receptor
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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
P16154
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Expression Region
2387-2710aa
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AA Sequence
ASTGYTSINGKHFYFNTDGIMQIGVFKGPNGFEYFAPANTDANNIEGQAILYQNKFLTLNGKKYYFGSDSKAVTGLRTIDGKKYYFNTNTAVAVTGWQTINGKKYYFNTNTSIASTGYTIISGKHFYFNTDGIMQIGVFKGPDGFEYFAPANTDANNIEGQAIRYQNRFLYLHDNIYYFGNNSKAATGWVTIDGNRYYFEPNTAMGANGYKTIDNKNFYFRNGLPQIGVFKGSNGFEYFAPANTDANNIEGQAIRYQNRFLHLLGKIYYFGNNSKAVTGWQTINGKVYYFMPDTAMAAAGGLFEIDGVIYFFGVDGVKAPGIYG
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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
Related Products
Protein Description
ToxA is a prominent protein associated with the pathogenicity of the plant pathogen *Pseudomonas syringae* pv. phaseolicola, responsible for bacterial blight in common bean plants. The study of ToxA has garnered interest due to its role as a key elicitor of plant defense responses, particularly in susceptible bean varieties. The protein is known to induce chlorosis and necrosis in host plants, making it a suitable model for investigating plant-pathogen interactions at the molecular level. Understanding the structure and function of ToxA is critical, as it can provide insights into the mechanisms of virulence employed by pathogens and the corresponding plant defenses. Recent advances in recombinant DNA technology have enabled the production of ToxA in heterologous systems, facilitating detailed studies on its biochemical properties and interactions with host plant receptors. Research into ToxA is not only relevant for enhancing our fundamental understanding of plant immunology but also holds potential for developing disease-resistant crops through targeted breeding or genetic engineering strategies. Additionally, exploring the conformation and functional domains of ToxA assists in uncovering its mode of action, which may lead to innovative approaches for managing bacterial diseases in agriculture. Thus, investigations surrounding ToxA as a recombinant protein represent a significant avenue for both basic and applied research in plant biology and crop protection.
