| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTM5 |
| Uniprot No | P46439 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-218aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMPMTLGYWDIRGLAHAIRLLLEYTDS SYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAI LRYIARKHNLCGETEEEKIRVDILENQVMDNHMELVRLCYDPDFEKLKPK YLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLD AFLNLKDFISRFEGLKKISAYMKSSQFLRGLLFGKSATWNSK |
| 预测分子量 | 28 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GSTM5重组蛋白的3篇示例参考文献(内容为模拟虚构，仅供参考格式)：
1. **文献名称**: "Expression and Functional Characterization of Recombinant Human GSTM5 in E. coli"
**作者**: Smith J, et al.
**摘要**: 研究通过大肠杆菌系统成功表达并纯化GSTM5重组蛋白，验证其对多种亲电底物的谷胱甘肽结合活性，揭示其底物特异性与酶动力学参数。
2. **文献名称**: "Crystal Structure of GSTM5 Reveals Unique Substrate-Binding Sites"
**作者**: Lee S, Kim M, et al.
**摘要**: 解析GSTM5重组蛋白的晶体结构，发现其活性位点与GSTM家族其他成员存在差异，提示其可能参与特定致癌代谢物的解毒机制。
3. **文献名称**: "Role of GSTM5 in Oxidative Stress: Insights from Recombinant Protein Studies"
**作者**: Wang Y, et al.
**摘要**: 利用重组GSTM5蛋白探究其在氧化应激中的作用，发现其通过调控ROS水平影响细胞凋亡通路，可能成为癌症治疗的潜在靶点。
注：以上文献为示例，实际研究中建议通过PubMed或Web of Science检索真实文献。
GSTM5 (Glutathione S-Transferase Mu 5) is a member of the glutathione S-transferase (GST) superfamily, a group of phase II detoxification enzymes that catalyze the conjugation of glutathione (GSH) to electrophilic substrates. This process neutralizes reactive toxins, oxidative stress byproducts, and carcinogens, facilitating their excretion. The Mu-class GSTs, including GSTM5. are primarily expressed in organs such as the liver, kidneys, and lungs, where detoxification is critical. GSTM5 shares structural homology with other Mu-class isoforms, featuring a conserved GSH-binding site and a hydrophobic substrate-binding domain. However, its specific substrate preferences and regulatory mechanisms remain less characterized compared to isoforms like GSTM1 or GSTM3.
Recombinant GSTM5 protein is produced using heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) to enable functional and structural studies. Its production typically involves cloning the GSTM5 gene into expression vectors, optimizing conditions for solubility and yield, and purifying the protein via affinity chromatography. Recombinant GSTM5 retains enzymatic activity, allowing researchers to study its role in cellular detoxification pathways, drug metabolism, and disease associations. For instance, polymorphisms in GST genes, including GSTM5. have been linked to cancer susceptibility, neurodegenerative disorders, and oxidative stress-related conditions.
Research on recombinant GSTM5 also explores its potential as a therapeutic target or biomarker. Its interaction with chemotherapeutic agents, environmental toxins, and signaling molecules highlights its relevance in pharmacology and toxicology. Structural analyses using recombinant protein help elucidate substrate specificity and design inhibitors to modulate its activity. Despite its lower abundance compared to other GSTs, GSTM5’s unique expression patterns and catalytic properties make it a subject of growing interest in precision medicine and molecular toxicology.
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