Analytical Data
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基因名
sepA
- Application
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别名
SEPP1
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种属
Staphylococcus epidermidis
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0C0Q4
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表达区间
208-507aa
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分子量
37.7 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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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
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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.
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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.
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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
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Protein Description
The study of sepA recombinant protein is rooted in the field of molecular biology and its applications in understanding bacterial pathogenesis. SepA, or secreted effector protein A, is a key component secreted by certain pathogens, such as *Pseudomonas aeruginosa*, which is known for its role in mediating virulence and modulating host immune responses. The ability of sepA to influence cellular pathways makes it a significant target for research focused on unraveling the mechanisms of infection and disease. Understanding how sepA functions at the molecular level can provide insights into the interactions between pathogens and host systems, potentially leading to the development of novel therapeutic strategies. The recombination technology allows researchers to produce this protein in a controlled environment, facilitating detailed studies of its structure and function. Furthermore, recombinant sepA can serve as a potential vaccine candidate or a tool for immunological studies, enhancing our understanding of host-pathogen dynamics. Therefore, investigating sepA recombinant protein is crucial for both basic research and applied sciences, contributing to the broader goal of controlling bacterial infections and improving public health outcomes.
