| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRS |
| Uniprot No | Q75006 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-107aa |
| 氨基酸序列 | MAGRSGDSDEELLKAVRIIKILYQSNPYPTPEGTRQARRNRRRRWRARQRQIHTLSERILSNFLGRPAEPVPLQLPPLERLNLDCSEDSGTSGTQQSQGTTEGVGNP |
| 预测分子量 | 38.7 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TRS重组蛋白的3篇参考文献的简要整理：
1. **文献名称**：*Mechanistic insights into the RNA recombination activity of the coronavirus TRS-containing protein*
**作者**：Smith J. et al.
**摘要**：研究揭示了冠状病毒中TRS(转录调控序列)重组蛋白在病毒RNA复制中的关键作用，发现其通过介导RNA链的跳跃和重组促进亚基因组RNA的生成。
2. **文献名称**：*Expression and purification of recombinant TRS protein in Escherichia coli for structural studies*
**作者**：Zhang L. et al.
**摘要**：报道了一种利用大肠杆菌表达系统高效表达TRS重组蛋白的方法，并通过亲和层析纯化获得高纯度蛋白，为后续结构解析奠定基础。
3. **文献名称**：*Functional analysis of TRS-mediated recombination in viral evolution and vaccine development*
**作者**：Gupta R. et al.
**摘要**：探讨了TRS重组蛋白在病毒进化中驱动基因多样性的机制，并验证了基于TRS重组的减毒疫苗设计策略的可行性。
(注：以上文献为示例性内容，实际引用需根据具体研究领域和数据库检索结果调整。)
TRS recombinant proteins are engineered molecules designed to mimic or modulate specific biological processes, often inspired by natural protein interactions. The term "TRS" commonly refers to Transcriptional Regulatory Sequences or Transmembrane Signaling Receptors in different contexts, but in recombinant protein research, it frequently relates to targeted receptor-binding domains or synthetic transcription-regulating elements. These proteins are typically developed using genetic engineering techniques, combining functional domains from native proteins with synthetic linkers or stabilization motifs to enhance stability, specificity, or therapeutic efficacy.
A prominent example involves TRS motifs derived from viral pathogens, such as the SARS-CoV-2 spike protein's receptor-binding domain (RBD). Recombinant TRS-based proteins have been critical in vaccine development, diagnostic tools, and therapeutic antibodies. They enable precise antigen presentation for immune activation or serve as decoy receptors to neutralize pathogens. Advanced expression systems (e.g., mammalian, insect, or yeast cells) ensure proper post-translational modifications, maintaining structural integrity for functional studies or clinical applications.
Research also explores TRS recombinant proteins in gene therapy, where they act as synthetic transcription factors to regulate gene expression. Their modular design allows customization for targeting specific DNA sequences or cellular pathways, offering potential treatments for genetic disorders or cancers. Challenges include optimizing delivery mechanisms, minimizing immunogenicity, and ensuring long-term stability in vivo. Ongoing innovations in protein engineering, such as fusion tags (e.g., Fc regions for extended half-life) or computational protein design, continue to expand their therapeutic and industrial applications, positioning TRS recombinant proteins as versatile tools in biotechnology and medicine.
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