| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | omcB |
| Uniprot No | P23700 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 41-196aa |
| 氨基酸序列 | SAETKPAPVPMTAKKVRLVRRNKQPVEQKSRGAFCDKEFYPCEEGRCQPVEAQQESCYGRLYSVKVNDDCNVEICQSVPEYATVGSPYPIEILAIGKKDCVDVVITQQLPCEAEFVSSDPETTPTSDGKLVWKIDRLGAGDKCKITVWVKPLKEGC |
| 预测分子量 | 24.2 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. |
以下是关于omcB重组蛋白的模拟参考文献示例(基于已知研究的概括，建议通过学术数据库核实具体文献)：
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1. **文献名称**：*Expression and purification of recombinant OMCB from Neisseria gonorrhoeae for structural analysis*
**作者**：Smith J, et al.
**摘要**：本研究在大肠杆菌中成功表达了淋病奈瑟菌的omcB重组蛋白，通过亲和层析纯化并分析了其结构。研究证实重组OMCB具有与天然蛋白相似的构象，为后续疫苗开发提供了基础。
2. **文献名称**：*Immunogenicity of a recombinant OMCB-based vaccine against bacterial infection*
**作者**：Lee H, et al.
**摘要**：通过克隆omcB基因并在哺乳动物细胞中表达重组蛋白，评估了其作为疫苗候选抗原的潜力。动物实验显示，重组OMCB可诱导强烈的Th1免疫应答，显著降低感染模型中的病原负荷。
3. **文献名称**：*Functional characterization of OMCB in bacterial outer membrane biogenesis*
**作者**：Zhang R, et al.
**摘要**：利用重组OMCB蛋白进行体外结合实验，揭示了其在细菌外膜组装中的作用机制。研究发现，OMCB与脂多糖(LPS)的相互作用对维持膜稳定性至关重要。
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注：以上文献为示例性概括，实际文献需通过PubMed、Web of Science等平台检索关键词(如“recombinant OMCB protein”、“omcB gene expression”)获取。
**Background of OmcB Recombinant Protein**
OmcB (outer membrane cytochrome B) is a key redox-active protein found in the outer membrane of certain Gram-negative bacteria, particularly in metal-reducing microorganisms like *Shewanella* and *Geobacter* species. These bacteria are notable for their ability to transfer electrons extracellularly, a process critical for respiration in anaerobic environments or during interactions with insoluble substrates such as Fe(III) oxides or electrodes. OmcB belongs to the multiheme cytochrome family, characterized by its β-barrel structure and multiple heme-binding sites, which facilitate electron transport across the membrane.
The interest in OmcB stems from its role in microbial extracellular electron transfer (EET), a mechanism with applications in bioenergy (e.g., microbial fuel cells), bioremediation of contaminated environments, and biogeochemical cycling of metals. Recombinant OmcB is produced via genetic engineering, where the *omcB* gene is cloned into expression vectors (e.g., *E. coli* systems) and purified for functional studies. This approach allows researchers to study its structural properties, redox behavior, and interactions with abiotic surfaces or microbial partners without interference from native cellular components.
Research on recombinant OmcB has provided insights into its potential as a bioelectrocatalyst, its role in nanowire formation for long-range electron transport, and its application in biosensors or biohybrid systems. Additionally, OmcB’s ability to interface with synthetic materials has spurred interest in bio-inspired nanotechnology and sustainable energy solutions. Understanding its molecular mechanisms also aids in engineering synthetic microbes for enhanced EET efficiency.
Overall, OmcB recombinant protein serves as a model for deciphering microbial electroactivity and bridging biological processes with technological innovations in environmental and energy sciences.
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