| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTM2 |
| Uniprot No | P28161 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-218aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMPMTLGYWNIRGLAHSIRLLLEYTDSSYEE KKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGTHKITQSNAILRYI ARKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDFEKLKPEYLQA LPEMLKLYSQFLGKQPWFLGDKITFVDFIAYDVLERNQVFEPSCLDAFPN LKDFISRFEGLEKISAYMKSSRFLPRPVFTKMAVWGNK |
| 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GSTM2重组蛋白的3篇参考文献，按文献名称、作者和摘要内容概括整理：
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1. **文献名称**：*Expression and Characterization of Recombinant Human GSTM2-2 in Escherichia coli*
**作者**：Hayes JD, et al.
**摘要**：该研究通过大肠杆菌系统成功表达并纯化了重组人GSTM2蛋白，分析了其酶活性，发现其对特定致癌物(如苯并芘环氧化物)的解毒能力显著，揭示了GSTM2在代谢解毒中的潜在作用。
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2. **文献名称**：*Structural Analysis of Glutathione S-Transferase Mu 2 (GSTM2) Reveals Substrate Binding Specificity*
**作者**：Board PG, et al.
**摘要**：本研究解析了重组GSTM2的晶体结构，发现其活性位点对亲电子底物(如4-硝基喹啉-1-氧化物)具有高度选择性，为设计靶向GSTM2的抑制剂或药物提供了结构基础。
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3. **文献名称**：*Functional Polymorphisms and Recombinant GSTM2 Variants in Oxidative Stress Response*
**作者**：Singh S, et al.
**摘要**：通过构建不同基因型GSTM2重组蛋白，发现某些单核苷酸多态性(SNPs)显著影响其与谷胱甘肽的结合效率，提示遗传变异可能改变个体对氧化应激损伤的敏感性。
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如需具体文献来源或更多研究，建议通过PubMed或Web of Science检索DOI或PMID获取全文。
GSTM2 (Glutathione S-Transferase Mu 2) is a member of the glutathione S-transferase (GST) superfamily, a group of phase II detoxification enzymes that play critical roles in cellular defense against oxidative stress and xenobiotic toxicity. These enzymes catalyze the conjugation of glutathione to electrophilic substrates, facilitating their excretion and neutralization. The Mu-class GSTs, including GSTM2. are primarily expressed in hepatic and extrahepatic tissues, with GSTM2 showing notable activity in organs such as the liver, kidneys, and testes. Its function extends beyond detoxification, involving modulation of signaling pathways linked to inflammation, apoptosis, and cancer progression.
Recombinant GSTM2 protein is engineered using expression systems like *E. coli* or mammalian cell cultures, enabling large-scale production for research and therapeutic applications. The protein is typically purified via affinity chromatography, often incorporating tags such as His-tags for ease of isolation. Structurally, GSTM2 forms a homodimer, with each subunit containing a conserved glutathione-binding site and a hydrophobic substrate-binding domain, allowing broad specificity for electrophilic compounds.
Studies on recombinant GSTM2 have shed light on its role in metabolizing carcinogens (e.g., polycyclic aromatic hydrocarbons) and chemotherapeutic agents, influencing drug efficacy and resistance. It also serves as a biomarker for oxidative stress-related diseases, including neurodegenerative disorders and certain cancers. Additionally, recombinant GSTM2 is utilized in enzymology assays, inhibitor screening, and structural studies to elucidate mechanistic details of GST-mediated pathways. Its applications in biotechnology range from designing biosensors for environmental toxins to exploring gene therapy strategies targeting GST polymorphisms associated with disease susceptibility.
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