Analytical Data
-
基因名
bepA
- Application
-
种属
Escherichia coli
-
表达系统
E. coli
-
标签
N- His & C- Myc
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P66948
-
表达区间
28-487aa
-
分子量
58.5 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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.












