| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTM1 |
| Uniprot No | P09488 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-181aa |
| 氨基酸序列 | MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEF EKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKGLEKISAYMKSSRFLPRPVFSKMAVWGN K |
| 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. |
以下是关于GSTM1重组蛋白的模拟参考文献示例(非真实文献，仅供格式参考)：
1. **文献名称**：*Expression and purification of recombinant human GSTM1 in Escherichia coli*
**作者**：Zhang, L., et al.
**摘要**：研究报道了通过大肠杆菌表达系统成功克隆并纯化人源GSTM1重组蛋白，优化了诱导条件以获得高溶解度蛋白，并验证其谷胱甘肽结合活性。
2. **文献名称**：*Functional characterization of GSTM1 polymorphism variants using recombinant protein analysis*
**作者**：Smith, J.D., & Wang, Y.
**摘要**：通过体外表达不同基因型(如GSTM1*null和GSTM1*active)的重组蛋白，分析其酶动力学差异，揭示特定突变对解毒功能的影响。
3. **文献名称**：*GSTM1 recombinant protein as a biomarker for oxidative stress in lung cancer*
**作者**：Chen, H., et al.
**摘要**：探讨重组GSTM1蛋白在肺癌细胞模型中的作用，证明其通过调节ROS水平抑制肿瘤生长，提示其作为治疗靶点的潜力。
4. **文献名称**：*Crystal structure and substrate specificity of recombinant GSTM1*
**作者**：Tanaka, K., et al.
**摘要**：解析GSTM1重组蛋白的晶体结构，结合分子对接实验阐明其底物结合口袋的构效关系，为设计特异性抑制剂提供依据。
**注意**：以上为生成的示例，实际文献需通过PubMed、Google Scholar等平台检索关键词“GSTM1 recombinant protein”“GSTM1 purification”或“GSTM1 enzyme activity”获取。
**Background of GSTM1 Recombinant Protein**
Glutathione S-transferase Mu 1 (GSTM1) is a critical enzyme in the glutathione S-transferase (GST) family, involved in cellular detoxification processes. It catalyzes the conjugation of glutathione to electrophilic compounds, facilitating the elimination of toxins, carcinogens, and oxidative stress byproducts. GSTM1 is predominantly expressed in the liver, kidneys, and lungs, playing a key role in phase II metabolism. Genetic polymorphisms in *GSTM1*, particularly the common null variant (deletion of the gene), have been linked to altered susceptibility to cancers, neurodegenerative diseases, and inflammatory conditions due to impaired detoxification capacity.
Recombinant GSTM1 protein is produced via heterologous expression systems, such as *E. coli* or mammalian cell lines, enabling large-scale purification for research and therapeutic applications. The recombinant form retains the native enzyme’s functional properties, including substrate binding and catalytic activity. Its structure typically includes conserved GST domains: an N-terminal thioredoxin-fold domain for glutathione binding and a C-terminal helical domain for hydrophobic substrate recognition.
In research, recombinant GSTM1 is widely used to study detoxification mechanisms, drug metabolism, and oxidative stress responses. It serves as a tool for screening potential chemopreventive agents or inhibitors, analyzing enzyme kinetics, and modeling genetic deficiencies. Additionally, it aids in structural studies (e.g., X-ray crystallography) to explore ligand interactions and mutation effects. In biotechnology, GSTM1 fusion tags are sometimes employed for protein purification via glutathione-affinity chromatography.
Overall, GSTM1 recombinant protein provides a versatile platform for understanding metabolic diseases, designing targeted therapies, and advancing toxicology research, bridging genetic insights with functional biochemistry.
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