Analytical Data
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Gene name
TalB
- Application
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Alternative Names
yaaK
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A870
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Expression Region
2-317aa
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Molecular Weight
42.5 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
TalB is a protein derived from the bacterium *Xanthomonas*, which has gained significant attention in the field of molecular biology and plant pathology. This protein is part of a larger family of type III secretion system effectors, known for manipulating host plant immune responses to facilitate bacterial infection. TalB specifically interacts with host signaling pathways to promote disease susceptibility, making it a crucial player in the virulence of *Xanthomonas* species. Researchers are increasingly interested in TalB due to its potential applications in developing disease-resistant crops through targeted manipulation of plant pathways. Additionally, studies into the structure and function of TalB can provide insights into the molecular mechanisms of host-pathogen interactions, contributing to our understanding of plant immunity. The advancements in genetic engineering techniques, such as CRISPR/Cas9, have further propelled research into TalB, allowing for precise modifications in both bacterial and plant genomes. Investigating TalB's interactions at the molecular level not only enhances our fundamental knowledge of plant-microbe interactions but also paves the way for innovative strategies to combat crop diseases and improve agricultural sustainability in the face of global food security challenges.
