Analytical Data
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基因名
omp1
- Application
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别名
Major outer membrane porin, serovar D; MOMP; ompA; omp1; CT_681
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种属
Others
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表达系统
E. coli
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标签
C-Myc;N-10*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q46409
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表达区间
L23-F393
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蛋白长度
Full Length of Mature Protein
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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
OMP1 (Outer Membrane Protein 1) is a significant protein primarily found in the outer membrane of certain Gram-negative bacteria, such as *Acinetobacter baumannii* and *Pseudomonas aeruginosa*. Its role in bacterial pathogenicity, including adherence to host tissues and evasion of the immune response, has made it a focal point of research in microbiology and infectious diseases. OMP1's structure and function are also of interest due to its potential as a vaccine candidate and a target for antibiotic development. The study of recombinant OMP1 enables researchers to explore its immunogenic properties, facilitating the design of vaccines that could provide protection against infections caused by these pathogens. Furthermore, the production of recombinant OMP1 in suitable expression systems allows for detailed structural and functional analyses, which can enhance our understanding of its interactions with host cells. Given the rising concern over antibiotic resistance and the urgency to develop novel therapeutic strategies, the investigation of OMP1 holds promise for contributing to the development of effective interventions against bacterial infections. Thus, research into OMP1 not only deepens scientific understanding but also has practical implications for public health.












