| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Trp |
| Uniprot No | P07477 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-247aa |
| 氨基酸序列 | IVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS |
| 预测分子量 | 26.9 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3篇与Trp重组蛋白相关的参考文献示例(注：文献信息为模拟生成，仅供参考)：
1. **文献名称**：Optimization of Recombinant Tryptophan Synthase Expression in E. coli
**作者**：Chen L., et al.
**摘要**：研究通过优化大肠杆菌表达系统中的诱导条件和培养基成分，显著提高了Trp重组蛋白的产量，并分析了温度与IPTG浓度对可溶性表达的影响。
2. **文献名称**：Structural Analysis of Tryptophan Repressor Protein-DNA Interaction
**作者**：Smith J.R., et al.
**摘要**：通过X射线晶体学解析了Trp重组蛋白与DNA结合的结构，揭示了其调控色氨酸生物合成相关基因的分子机制及关键氨基酸残基的作用。
3. **文献名称**：Application of Recombinant Trp Operon Proteins in Metabolic Engineering
**作者**：Wang Y., et al.
**摘要**：探讨了利用重组Trp操纵子蛋白(如TrpE、TrpD)构建微生物细胞工厂的策略，成功提高了色氨酸的合成效率，为工业发酵提供新思路。
建议通过PubMed、Web of Science或Google Scholar检索关键词如 "recombinant tryptophan protein" 或 "Trp operon expression" 获取真实文献。
**Background of Trp Recombinant Proteins**
Trp (tryptophan) recombinant proteins are engineered polypeptides that incorporate tryptophan residues at specific positions or are derived from Trp-rich domains of natural proteins. Tryptophan, an essential aromatic amino acid, plays critical roles in protein structure and function due to its unique indole side chain, which contributes to hydrophobic interactions, π-stacking, and fluorescence properties. These characteristics make Trp residues valuable in studying protein folding, stability, and molecular interactions.
Recombinant Trp proteins are typically produced via genetic engineering, where target genes are cloned into expression vectors and expressed in host systems (e.g., *E. coli*, yeast, or mammalian cells*). The inclusion of Trp-rich motifs or tags (e.g., Trp “affinity” tags) can enhance protein solubility, facilitate purification, or serve as reporters in spectroscopic analyses. For instance, Trp fluorescence is widely used to monitor conformational changes in proteins during ligand binding or denaturation.
Trp-rich domains are also found in natural antimicrobial peptides (AMPs) and viral fusion proteins, where their hydrophobicity and structural rigidity mediate membrane interactions. Recombinant versions of these proteins are pivotal in developing antimicrobial agents or studying viral entry mechanisms. Additionally, Trp auxotrophy in certain expression systems allows selective labeling with isotopic or fluorescent Trp analogs, enabling advanced techniques like nuclear magnetic resonance (NMR) or Förster resonance energy transfer (FRET).
Despite their utility, producing functional Trp recombinant proteins can face challenges, such as host toxicity from overexpressed hydrophobic sequences or misfolding. Optimization of expression conditions, codon usage, and purification strategies is often required.
Overall, Trp recombinant proteins serve as versatile tools in biochemistry, structural biology, and therapeutic development, leveraging the unique properties of tryptophan to advance both fundamental research and biotechnological applications.
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