| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | rne |
| Uniprot No | P21513 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-125aa |
| 氨基酸序列 | EQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPANYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGS |
| 预测分子量 | 16.1 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RNE重组蛋白的假设性参考文献示例(注：RNE蛋白的具体定义可能存在差异，建议结合具体研究领域进一步检索)：
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1. **文献名称**: *"High-yield production of recombinant RNE protein in E. coli for structural studies"*
**作者**: Müller, J., et al.
**摘要**: 本研究开发了一种高效的大肠杆菌表达系统，用于生产具有活性的重组RNE蛋白。通过优化表达条件和纯化步骤，获得了高纯度蛋白，并利用X射线晶体学初步解析了其结构，为后续功能研究奠定基础。
2. **文献名称**: *"RNE recombinant protein exhibits RNA chaperone activity in vitro"*
**作者**: Chen, L., & Wang, H.
**摘要**: 通过体外实验证实重组RNE蛋白能够促进RNA分子的正确折叠，并参与RNA-蛋白质复合物的组装。研究揭示了RNE在RNA代谢中的多重功能，提示其可能应用于基因表达调控工具的开发。
3. **文献名称**: *"Targeted inhibition of viral replication using engineered RNE recombinant protein"*
**作者**: Gupta, R., et al.
**摘要**: 利用基因工程技术改造RNE蛋白，使其特异性识别并降解某RNA病毒的基因组。实验证明重组RNE显著抑制病毒复制，为抗病毒治疗提供了新策略。
4. **文献名称**: *"Functional interaction between RNE and helicases in bacterial stress response"*
**作者**: Tanaka, K., et al.
**摘要**: 通过重组RNE蛋白与解旋酶的共纯化实验，揭示了二者在细菌应激反应中的协同作用，阐明了RNE在RNA质量控制网络中的关键地位。
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**注意**：以上文献为示例性内容，实际研究中请通过学术数据库(如PubMed、Web of Science)以**“RNE protein recombinant”**或结合具体物种/功能(如“RNase E recombinant”)为关键词检索最新文献。若RNE指代特定基因(如rne基因)，需进一步明确生物学背景。
RNE recombinant protein, often associated with advanced biotechnological applications, is engineered through recombinant DNA technology to produce specific protein variants with enhanced stability, solubility, or functional properties. The term "RNE" may refer to a protein of interest in specific research or industrial contexts, such as a therapeutic target, enzymatic tool, or diagnostic marker. Recombinant proteins, in general, are generated by inserting a gene encoding the desired protein into a host organism (e.g., bacteria, yeast, or mammalian cells), which then expresses the protein for purification and use.
The development of RNE recombinant protein likely stems from the need to overcome limitations of native proteins, such as low yield, structural instability, or post-translational modification requirements. For instance, if RNE is an enzyme or receptor involved in critical cellular processes, its recombinant form could enable large-scale production for drug discovery, structural studies, or biomanufacturing. Applications may span therapeutics (e.g., monoclonal antibodies, vaccines), industrial biocatalysis, or research tools for studying molecular pathways.
Advances in protein engineering, including codon optimization, fusion tags, and expression system optimization, have facilitated the production of RNE recombinant variants with tailored characteristics. For example, fusion partners like His-tags or GST-tags may enhance purification efficiency, while site-directed mutagenesis could improve thermal stability or catalytic activity. Quality control assays (e.g., SDS-PAGE, Western blot, functional assays) ensure batch consistency and bioactivity.
RNE recombinant proteins may also play roles in personalized medicine or biopharmaceuticals, aligning with trends in precision therapeutics. Challenges include minimizing host-induced heterogeneity (e.g., glycosylation differences) and scaling production cost-effectively. Overall, RNE recombinant protein exemplifies the intersection of molecular biology and industrial innovation, addressing diverse needs in healthcare, biotechnology, and scientific research.
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