| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GST |
| Uniprot No | O43916 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 168-267aa |
| 氨基酸序列 | PPGPADLVLEEGDCVRKCGLLNLTVAAEACRERSHVAIKTVRVPEVNDLR ALVEDPRLNLKVIQLVRDPRGILASRSETFRDTYRLWRLWYGTGRKPYNL |
| 预测分子量 | 37 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3-4条关于GST重组蛋白的经典参考文献，按发表时间排序：
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1. **文献名称**：*Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase*
**作者**：Smith, D. B., & Johnson, K. S.
**摘要**：提出利用GST(谷胱甘肽S-转移酶)作为融合标签的重组蛋白表达系统(pGEX载体)，通过谷胱甘肽亲和层析实现一步纯化，显著简化了蛋白纯化流程。
2. **文献名称**：*Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins*
**作者**：Frangioni, J. V., & Neel, B. G.
**摘要**：系统分析GST融合蛋白在大肠杆菌中的表达条件、溶解性优化策略，以及如何通过调整缓冲液成分和纯化步骤提高蛋白回收率。
3. **文献名称**：*GST affinity fusion system: Design and applications*(收录于书籍 *Protein Purification Techniques*)
**作者**：Harper, S., & Speicher, D. W.
**摘要**：综述GST标签技术的原理、载体设计及在蛋白相互作用研究(如Pull-down实验)中的应用，提供详细实验方案和常见问题解决方案。
4. **文献名称**：*Optimization of GST protein expression in E. coli: Effect of induction temperature and culture media*
**作者**：Buchwald, P., et al.
**摘要**：探讨不同诱导温度、培养基成分对GST重组蛋白可溶性表达的影响，提出优化策略以提高产量并减少包涵体形成。
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**注**：以上文献均为GST标签技术领域的代表性研究，涵盖表达、纯化和优化策略，适用于重组蛋白制备及功能研究。
**Background of GST-Tagged Recomcombinant Proteins**
Glutathione S-transferase (GST) is a 26-kDa enzyme originally identified in the parasitic flatworm *Schistosoma japonicum*. In the 1980s, GST was adapted as a fusion tag for recombinant protein expression and purification, driven by its high-affinity binding to glutathione, a tripeptide antioxidant. This property led to the development of the GST gene fusion system, a cornerstone of affinity chromatography.
The GST tag serves dual purposes: it enhances solubility and stability of recombinant proteins during expression in bacterial (e.g., *E. coli*) or eukaryotic systems, while enabling rapid purification via glutathione-coated beads. The system, pioneered by Smith and Johnson in 1988. involves cloning a target gene into a GST-fusion vector (e.g., pGEX). Upon expression, the GST-tagged protein binds to immobilized glutathione matrices under mild conditions. Impurities are washed away, and the purified fusion protein is eluted using reduced glutathione or enzymatic cleavage.
GST-tagged proteins are widely used in pull-down assays, protein-protein interaction studies, and antibody production. The tag’s large size can sometimes interfere with protein function, necessitating tag removal via proteases like thrombin or PreScission. Despite the emergence of smaller tags (e.g., His-tag), GST remains popular due to its efficient purification, compatibility with diverse expression systems, and utility in immobilizing proteins for interaction screens or drug discovery.
Today, GST fusion technology is a staple in structural biology, proteomics, and biotechnology, balancing simplicity, cost-effectiveness, and versatility for routine or large-scale protein production.
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