Analytical Data
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Gene name
peb1A
- Application
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Alternative Names
CBF1 PEB1
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Species
strain 81-176
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A1VZQ4
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Expression Region
27-259aa
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Molecular Weight
45.4 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
PEB1A (Pathogen Effector Protein 1A) is a key protein secreted by pathogenic bacteria, particularly those involved in plant diseases, playing a crucial role in plant-pathogen interactions. Its study has garnered significant attention due to its potential impact on agriculture and food security, as understanding the mechanisms by which PEB1A manipulates plant immune responses could lead to the development of more resilient crop varieties. Research has shown that PEB1A functions by targeting specific plant proteins, altering their normal functions, and thereby suppressing the plant's defense mechanisms. This manipulation enables the pathogen to establish infection and thrive within the host. Moreover, the investigation into PEB1A's structure and functional domains offers insights into general strategies employed by pathogens to evade host defenses. With the increasing challenges posed by climate change and emerging diseases, the exploration of PEB1A and similar proteins is critical for developing novel biotechnological approaches and crop protection strategies, ultimately contributing to sustainable agriculture practices. Understanding PEB1A and its interactions provides a vital step toward devising new ways to combat plant pathogens and enhance crop resilience, highlighting the need for continued research in this area.
