| 纯度 | >95%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | TST |
| Uniprot No | P0A6V5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-108aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMDQFECI NVADAHQKLQ EKEAVLVDIR DPQSFAMGHA VQAFHLTNDT LGAFMRDNDF DTPVMVMCYH GNSSKGAAQY LLQQGYDVVY SIDGGFEAWQ RQFPAEVAYG A |
| 预测分子量 | 15 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. |
以下是为您模拟的3篇关于TST(假设为结核菌素皮肤试验相关)重组蛋白的参考文献示例。请注意，这些文献为虚构内容，仅作格式参考：
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1. **文献名称**：Expression and Purification of Recombinant TST Fusion Protein for Tuberculosis Diagnosis
**作者**：Zhang L. et al.
**摘要**：本研究利用大肠杆菌表达系统成功制备了TST重组融合蛋白，通过亲和层析纯化获得高纯度产物。Western blot验证显示该蛋白可与结核患者血清特异性结合，为开发新型诊断试剂奠定基础。
2. **文献名称**：Evaluation of Recombinant TST Protein Sensitivity in Latent TB Detection
**作者**：Smith J.R., Patel K.
**摘要**：团队将重组TST蛋白应用于ELISA检测，对比传统PPD试剂。结果显示，重组蛋白对潜伏性结核的检测灵敏度达92%，且与BCG疫苗接种无交叉反应，显著提升诊断特异性。
3. **文献名称**：TST Recombinant Protein-Based Skin Test: A Phase I Clinical Trial
**作者**：Wang Y. et al.
**摘要**：首次在人体中评估重组TST蛋白的安全性。试验表明，低剂量皮内注射无严重不良反应，且能有效区分活动性结核与健康人群，支持其作为新一代结核菌素替代品的潜力。
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**说明**：
- 实际文献需通过PubMed、Web of Science等平台检索关键词(如“Recombinant TST protein”、“Tuberculin recombinant”)。
- 若TST指代其他蛋白(如硫转运蛋白)，请提供更多背景信息以便调整检索方向。
**Background of TST Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are pivotal in modern biotechnology and medicine. TST (a hypothetical designation for illustrative purposes) recombinant proteins represent a class of such molecules produced via advanced expression systems. These proteins are synthesized by inserting target genes into host organisms (e.g., bacteria, yeast, or mammalian cells), enabling large-scale production of specific proteins with tailored functions.
The development of recombinant protein technology emerged in the 1970s, driven by breakthroughs in molecular cloning and gene expression. TST recombinant proteins, as a subset, often emphasize optimized design for enhanced stability, solubility, or bioactivity. For instance, codon optimization of the target gene, fusion tags (e.g., His-tag, GST), or specialized promoters may be employed to boost expression efficiency in host systems like *E. coli* or CHO cells.
Applications span therapeutics, diagnostics, and research. TST recombinant proteins may serve as vaccines (e.g., subunit vaccines), therapeutic agents (e.g., monoclonal antibodies, cytokines), or tools for studying protein interactions and signaling pathways. Their clinical relevance is underscored by roles in treating cancers, autoimmune diseases, and infectious disorders.
Advantages over traditional protein extraction include scalability, reduced contamination risks, and precise customization. Challenges, such as improper folding or post-translational modification limitations in prokaryotic systems, are addressed through advanced expression platforms (e.g., mammalian or insect cells) or refolding techniques.
Recent innovations focus on improving yield, reducing costs, and enhancing functional accuracy via AI-driven protein design or CRISPR-edited host strains. TST recombinant proteins exemplify the intersection of genetic engineering and industrial biotechnology, offering transformative potential across healthcare and biomanufacturing.
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