Analytical Data
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Gene name
bopE
- Application
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Alternative Names
Effector protein BopE
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Species
Burkholderia mallei
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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
Q62B14
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Expression Region
1-261aa
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Molecular Weight
44.7 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
BopE, a type III secretion system (T3SS) effector protein secreted by the bacterial pathogen Burkholderia pseudomallei, has garnered significant attention in the field of infectious disease research due to its role in immune evasion and pathogenicity. As an important virulence factor, BopE modulates host cell signaling pathways, promoting bacterial survival and replication within host tissues. This protein has been implicated in disrupting the host's immune responses, including the manipulation of cellular processes such as apoptosis and inflammatory signaling. Given the increasing global burden of Burkholderia pseudomallei infections, particularly in endemic regions, understanding the mechanisms by which BopE contributes to the bacterium's virulence is critical. Research into BopE's structure, function, and interaction with host proteins could provide insights into novel therapeutic targets and strategies to combat infections caused by this opportunistic pathogen. Additionally, the study of BopE contributes to the broader understanding of T3SS effector proteins and their roles in microbial pathogenesis, underscoring the importance of this research in designing effective vaccines and treatment regimens against related bacterial infections.
