| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | trhO |
| Uniprot No | Q252M0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-325aa |
| 氨基酸序列 | MKKNYYALAYYHFTRVDNPQEEIALHKELFKKLDVSCRIYISEQGINGQFSGYQPDAEYYMNWLKQRPGFSNVKFKIHHIEENIFPRATVKYRKELVALGCDVDLSNQGKHISPKEWHEKLEENRCLVLDVRNNYEWKIGHFENAVLPDIQTFREFPEYAEQLSKEHDPETTPVMMYCTGGIRCELYSSLLLEKGFKEVYQLDGGVIAYGQAMGTGKWRGKLFVFDDRLAVPIDEADTDVSPIAQCSHCEASCDTYYNCANTDCNNLFICCEECIHSTKGCCSQECSQAPRIRSFSTSRGNKPFRRMHLCEISEEQEKPLSCCLR |
| 预测分子量 | 43.6 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trhO重组蛋白的3篇模拟参考文献(内容为学术场景假设，建议通过数据库查询真实文献)：
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1. **文献名称**: *Functional Characterization of trhO-Encoded Transport Protein in Halomonas titanicae*
**作者**: Zhang, L. et al.
**摘要**: 本研究在大肠杆菌中重组表达了Halomonas titanicae的trhO基因，证实其编码一种渗透压调节相关的转运蛋白，可促进四氢嘧啶(ectoine)的摄取，增强宿主在高盐环境下的生存能力。
2. **文献名称**: *Crystallization and Enzymatic Analysis of Recombinant trhO Protein from Pseudomonas aeruginosa*
**作者**: Wang, Y. & Kim, S.
**摘要**: 通过原核表达系统纯化获得trhO重组蛋白，酶活实验表明其具有水解特定嘧啶衍生物的活性，晶体结构解析揭示了其催化活性中心的关键氨基酸残基。
3. **文献名称**: *Role of trhO in Bacterial Virulence: Insights from Recombinant Protein Knockout Models*
**作者**: Gupta, R. et al.
**摘要**: 构建trhO基因缺失的突变菌株，发现trhO重组蛋白的缺失显著降低病原菌在宿主体内的定殖能力，表明其通过调控毒素分泌参与致病过程。
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如需实际文献，建议通过**PubMed/Google Scholar**检索关键词：
`trhO recombinant protein expression` 或 `trhO gene function`。
**Background of trhO Recombinant Protein**
The trhO recombinant protein is derived from the *trhO* gene, initially identified in pathogenic bacteria such as *Vibrio parahaemolyticus* and related species. This gene encodes an outer membrane protein involved in iron acquisition, a critical process for bacterial survival and virulence within host environments. trhO belongs to the TonB-dependent receptor family, which facilitates the uptake of iron-bound molecules (e.g., siderophores or heme) across the bacterial outer membrane by coupling with the TonB-ExbBD energy transduction system.
Iron limitation is a common challenge for pathogens during infection, making trhO essential for bacterial adaptation to host iron-restricted conditions. Studies suggest that trhO contributes to pathogenicity by enhancing bacterial iron scavenging, thereby promoting colonization and persistence in the host. Its role in virulence has drawn attention as a potential target for antimicrobial strategies or vaccine development.
Recombinant trhO is typically produced via heterologous expression in *Escherichia coli* systems, enabling large-scale purification for functional and structural studies. Characterization of the protein has revealed insights into its receptor-ligand interactions, conformational dynamics, and role in microbial iron metabolism. Additionally, recombinant trhO serves as an antigen in serodiagnostic assays to detect infections caused by *Vibrio* species, leveraging its immunogenic properties.
Research on trhO also explores its application in synthetic biology and bioremediation, given its ability to bind specific metal ions. However, challenges remain in optimizing expression yields and stability due to its membrane protein nature. Overall, trhO exemplifies a multifunctional bacterial protein with implications for understanding pathogenicity, host-pathogen interactions, and biotechnological innovation.
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