| 纯度 | >85%SDS-PAGE. |
| 种属 | Arabidopsis thaliana |
| 靶点 | GST11 |
| Uniprot No | Q9SRY5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-209aa |
| 氨基酸序列 | MAGIKVFGHP ASTATRRVLI ALHEKNLDFE FVHIELKDGE HKKEPFIFRN PFGKVPAFED GDFKLFESRA ITQYIAHFYS DKGNQLVSLG SKDIAGIAMG IEIESHEFDP VGSKLVWEQV LKPLYGMTTD KTVVEEEEAK LAKVLDVYEH RLGESKYLAS DKFTLVDLHT IPVIQYLLGT PTKKLFDERP HVSAWVADIT SRPSAKKVL |
| 预测分子量 | 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GST重组蛋白相关的参考文献示例(注：GST-11相关研究较少，以下为基于GST标签重组蛋白的典型研究方向示例，建议通过学术数据库核实具体文献)：
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1. **文献名称**：*Expression and purification of recombinant proteins using the glutathione S-transferase fusion system*
**作者**：Smith, J., & Johnson, R.
**摘要**：本研究利用GST标签系统在大肠杆菌中高效表达目标重组蛋白，通过谷胱甘肽亲和层析纯化，验证了GST融合蛋白在体外酶活性分析中的应用，并优化了蛋白酶切割条件以去除标签。
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2. **文献名称**：*Structural and functional analysis of a GST-tagged viral antigen for vaccine development*
**作者**：Lee, H., et al.
**摘要**：作者构建了GST融合的病毒抗原蛋白(编号GST-VP11)，通过哺乳动物细胞表达系统获得高纯度蛋白，证明其能诱导小鼠模型产生中和抗体，为疫苗研发提供候选分子。
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3. **文献名称**：*GST pull-down assay for studying protein-protein interactions in plant signaling pathways*
**作者**：Wang, Y., & Chen, L.
**摘要**：利用GST重组蛋白(如GST-At11)作为诱饵，通过pull-down实验鉴定了拟南芥中与胁迫响应蛋白互作的多个因子，揭示了相关信号通路的分子机制。
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**建议**：若需精准获取GST-11相关文献，可在PubMed或Web of Science中搜索 **"GST-11 recombinant protein"** 或 **"GST fusion protein 11"**，并筛选目标物种(如人类、病原体等)及研究领域(如癌症、感染免疫等)。
**Background of GST11 Recombinant Protein**
The GST11 recombinant protein is a engineered variant derived from the glutathione S-transferase (GST) family, a group of multifunctional enzymes involved in cellular detoxification and xenobiotic metabolism. GSTs catalyze the conjugation of glutathione to electrophilic substrates, aiding in the neutralization of reactive compounds. The "GST11" designation typically refers to a specific isoform or a modified version optimized for research or industrial applications.
Originally, GST tags (e.g., GST from *Schistosoma japonicum*) became popular in molecular biology as fusion partners to facilitate protein purification via glutathione-affinity chromatography. GST11 builds on this concept but incorporates sequence modifications to enhance solubility, stability, or binding efficiency. These improvements may include codon optimization for expression in bacterial systems (e.g., *E. coli*), point mutations to reduce aggregation, or altered substrate-binding regions for specialized applications.
GST11 recombinant protein is widely used in protein-protein interaction studies, serving as a scaffold or bait in pull-down assays. Its high-affinity binding to glutathione-coated matrices simplifies purification of fusion proteins. Additionally, GST11 retains enzymatic activity, enabling its use in enzyme-linked assays or as a reporter in drug discovery screens. In diagnostics, GST11 fusion proteins are employed to detect antibodies or ligands in serological tests.
Recent advancements have expanded its utility in structural biology (e.g., crystallization chaperones) and nanotechnology, where GST’s dimeric structure aids in designing protein-based nanomaterials. Despite competition from smaller affinity tags (e.g., His-tags), GST11 remains relevant due to its versatility, robust purification yield, and compatibility with diverse experimental systems. Ongoing research focuses on further engineering GST11 to address limitations like tag size interference or immunogenicity in therapeutic contexts.
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