| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTM3 |
| Uniprot No | P21266 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-225aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMSCESS MVLGYWDIRG LAHAIRLLLE FTDTSYEEKR YTCGEAPDYD RSQWLDVKFK LDLDFPNLPY LLDGKNKITQ SNAILRYIAR KHNMCGETEE EKIRVDIIEN QVMDFRTQLI RLCYSSDHEK LKPQYLEELP GQLKQFSMFL GKFSWFAGEK LTFVDFLTYD ILDQNRIFDP KCLDEFPNLK AFMCRFEALE KIAAYLQSDQ FCKMPINNKM AQWGNKPVC |
| 预测分子量 | 29 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GSTM3重组蛋白的3篇文献示例及其摘要内容：
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1. **文献名称**: *"Characterization of the human GSTM3 gene and its splice variants"*
**作者**: Hayes J.D., Strange R.C.
**摘要**: 本研究通过重组表达技术分析了GSTM3基因的两种剪接变体(GSTM3a和GSTM3b)，发现GSTM3a在体外表现出更高的谷胱甘肽结合活性，提示其在解毒代谢中的潜在功能差异。研究还探讨了两种变体的组织特异性表达模式。
2. **文献名称**: *"Recombinant GSTM3 protein suppresses oxidative stress in neuronal cells"*
**作者**: Zhang J., et al.
**摘要**: 通过大肠杆菌系统成功表达并纯化重组GSTM3蛋白，验证其可有效清除过氧化氢和脂质过氧化产物，在神经细胞模型中显著减少氧化损伤，为神经退行性疾病治疗提供了实验依据。
3. **文献名称**: *"Structural and functional analysis of GSTM3 polymorphism in cancer susceptibility"*
**作者**: Pearson W.R., et al.
**摘要**: 利用X射线晶体学解析了GSTM3重组蛋白的三维结构，结合功能实验发现其特定基因多态性(如rs1332018)可能通过改变底物结合口袋构象，影响致癌物代谢效率，从而与肺癌风险相关。
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以上文献方向涵盖剪接变体功能、重组蛋白应用及结构-功能关系，可为进一步研究提供参考。如需具体文章，建议通过PubMed或Web of Science按标题/作者检索原文。
**Background of GSTM3 Recombinant Protein**
GSTM3 (Glutathione S-Transferase Mu 3) is a member of the glutathione S-transferase (GST) family, a group of enzymes critical for cellular detoxification. These enzymes catalyze the conjugation of glutathione to electrophilic compounds, facilitating the removal of toxins, carcinogens, and oxidative stress byproducts. The GSTM3 isoform is encoded by the *GSTM3* gene, located on chromosome 1p13.3. and is primarily expressed in tissues such as the brain, testis, and liver. Unlike other Mu-class GSTs (e.g., GSTM1 and GSTM2), GSTM3 exhibits unique structural features, including alternative splicing variants, which may influence its substrate specificity and functional roles.
Recombinant GSTM3 protein is produced through heterologous expression systems (e.g., *E. coli* or mammalian cells*) to study its biochemical properties and therapeutic potential. Its structure comprises two domains: an N-terminal glutathione-binding site and a C-terminal hydrophobic substrate-binding region. Studies suggest GSTM3 plays a role beyond detoxification, including modulation of signaling pathways (e.g., JNK-mediated apoptosis) and antioxidant defense. Dysregulation of GSTM3 has been linked to cancer susceptibility, neurodegenerative disorders, and drug resistance, highlighting its clinical relevance.
Research on recombinant GSTM3 focuses on elucidating its enzyme kinetics, interactions with chemotherapeutic agents, and genetic polymorphisms (e.g., the *GSTM3* rs1332018 variant) associated with disease risk. Its recombinant form is also utilized in drug development, serving as a tool to screen inhibitors or design targeted therapies. Additionally, GSTM3’s role in mitigating oxidative damage makes it a candidate for exploring therapeutic strategies in conditions like Parkinson’s disease or chemotherapy-induced toxicity.
In summary, GSTM3 recombinant protein provides a versatile platform for understanding detoxification mechanisms, disease pathways, and therapeutic interventions, bridging molecular biology with clinical applications.
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