Analytical Data
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Gene name
bepA
- Application
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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
P66948
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Expression Region
28-487aa
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Molecular Weight
58.5 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
Related Products
Protein Description
The research on the recombinant protein BEP A (Bacterial Exotoxin Protein A) has gained significant attention due to its potential applications in various fields, particularly in therapeutics and biotechnology. BEP A is known for its role in the pathogenicity of certain bacteria, where it contributes to immune evasion and host cell manipulation. Understanding the structure and function of BEP A can provide insights into bacterial virulence mechanisms and reveal targets for the development of novel antimicrobial therapies. Additionally, the ability to produce BEP A in a recombinant form allows for detailed studies of its biochemical properties and interactions with host cells, which can be crucial in designing effective vaccines or immunotherapies. The manipulation of BEP A also holds promise in biotechnology, as it can be engineered for use in drug delivery systems or as a tool for targeted therapy. Researchers are utilizing advanced techniques such as molecular cloning, expression in host systems like Escherichia coli, and various purification methods to obtain sufficient quantities of this protein for in-depth analysis. The ongoing investigations into BEP A not only aim to enhance our understanding of bacterial pathogenesis but also to leverage its unique properties for innovative applications in medicine and biotechnology, making it a vital focus of contemporary microbiological and biochemical research.
