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Recombinant E.coli ompS1 protein

  • 中文名: 伤寒沙门氏菌外膜蛋白S1(ompS1)重组蛋白
  • 别    名: ompS1;ompS;Outer membrane protein S1
货号: PA2000-3109
Price: ¥询价
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纯度>90%SDS-PAGE.
种属 E.coli
靶点ompS1
Uniprot No Q56110
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 22-394aa
氨基酸序列AEIYNKNGNKLDLYGKVDGLRYFSDNAGDDGDQSYARIGFKGETQINDMLTGYGQWEYNIKVNTTEGEGANSWTRLGFAGLKFGEYGSFDYGRNYGVIYDIEAWTDALPEFGGDTYTQTDVYMLGRTNGVATYRNTDFFGLVEGLNFALQYQGNNENGGAGAGEGTGNGGNRKLARENGDGFGMSTSYDFDFGLSLGAAYSSSDRSDNQVARGYGDGMNERNNYAGGETAEAWTIGAKYDAYNVYLAAMYAETRNMTYYGGGNGEGNGSIANKTQNFEVVAQYQFDFGLRPSIAYLQSKGKDLGGQEVHRGNWRYTDKDLVKYVDVGMTYYFNKNMSTYVDYKINLLDEDDDFYANNGIATDDIVGVGLVYQF
预测分子量 57.2 kDa
蛋白标签His tag N-Terminus
缓冲液PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
稳定性 & 储存条件Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
复溶Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

参考文献

以下是关于ompS1重组蛋白的模拟参考文献示例(实际文献需通过学术数据库检索):

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1. **"Cloning and Expression of the ompS1 Gene from Salmonella Typhi in Escherichia coli"**

*Author: Lee, J. et al. (2010)*

**摘要**:本研究成功克隆伤寒沙门氏菌的ompS1基因,并在大肠杆菌中实现高效重组表达。通过SDS-PAGE和Western blot验证蛋白表达,并证实重组ompS1具有免疫原性,可能作为疫苗候选分子。

2. **"Structural Characterization of Recombinant OmpS1: Insights into Porin Function"**

*Author: Smith, R. et al. (2015)*

**摘要**:利用X射线晶体学解析重组OmpS1的三维结构,揭示其β-桶状孔蛋白特征及跨膜通道特性。研究还探讨了该蛋白在细菌感染过程中可能参与的宿主-病原体相互作用。

3. **"Evaluation of Recombinant OmpS1 as a Diagnostic Antigen for Typhoid Fever"**

*Author: Kumar, A. et al. (2020)*

**摘要**:将重组OmpS1作为抗原用于伤寒血清学检测,证实其与患者血清抗体反应的高灵敏度和特异性,表明其在开发快速诊断试剂中的潜在应用价值。

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**提示**:以上为示例文献,实际研究中建议通过PubMed、Google Scholar等平台以关键词“ompS1 recombinant protein”“Salmonella Typhi OmpS1”等检索最新论文。关注涉及基因表达、蛋白纯化、结构功能或免疫应用的研究。

背景信息

OmpS1 is a recombinant protein derived from the outer membrane protein S1 (OmpS1) of *Escherichia coli*, a member of the porin family. Porins are β-barrel transmembrane proteins that facilitate the passive diffusion of small hydrophilic molecules across the outer membrane of Gram-negative bacteria. OmpS1. specifically, forms trimeric channels with a characteristic β-barrel structure, allowing selective permeability based on size and charge. Its native role involves nutrient uptake, waste excretion, and maintaining membrane integrity, which is critical for bacterial survival in diverse environments.

Recombinant OmpS1 is engineered using genetic cloning techniques, where the *ompS1* gene is inserted into expression vectors (e.g., plasmids) and produced in heterologous hosts like *E. coli* or yeast. Purification typically involves affinity chromatography (e.g., His-tag systems) and refolding steps to ensure proper tertiary structure. The recombinant version retains key functional and structural features of the native protein, making it a valuable tool for structural biology studies, such as X-ray crystallography or cryo-EM, to elucidate pore-forming mechanisms and substrate specificity.

Research on OmpS1 has broader implications. It serves as a model for understanding bacterial membrane protein biogenesis and antibiotic resistance mechanisms, as porins often mediate drug influx/efflux. Additionally, its stability and modularity have sparked interest in biotechnological applications, including vaccine development (as an antigen or adjuvant carrier) and nanotechnology (e.g., synthetic nanopores for biosensing). Studies also explore its potential in drug delivery systems due to its ability to self-assemble into membrane-like structures.

Overall, OmpS1 recombinant protein bridges fundamental microbiology and applied science, offering insights into bacterial physiology while enabling innovations in therapeutics and bioengineering. Its simplicity, scalability, and functional versatility continue to make it a focal point in interdisciplinary research.

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