| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTA1 |
| Uniprot No | P08263 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-222aa |
| 氨基酸序列 | MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA DLGEMILLLP VCPPEEKDAK LALIKEKIKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEEARKIF RF |
| 预测分子量 | 27 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GSTA1重组蛋白的3篇代表性文献及其摘要概括：
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1. **标题**: "Expression and Characterization of Human Glutathione S-Transferase A1-1 in Escherichia coli"
**作者**: Hayes, J.D., et al.
**摘要**: 该研究通过大肠杆菌表达系统成功重组表达了人源GSTA1蛋白，并优化了纯化步骤(谷胱甘肽亲和层析)。研究发现重组GSTA1对脂质过氧化产物(如4-HNE)具有高催化活性，验证了其在解毒氧化应激中的作用。
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2. **标题**: "Structural Basis for Substrate Specificity of Glutathione S-Transferase A1-1"
**作者**: Oakley, A.J., et al.
**摘要**: 通过X射线晶体学解析了重组GSTA1的3D结构，揭示了其底物结合口袋的关键氨基酸残基。实验表明，GSTA1对亲电性化合物的选择性与其疏水通道的构象变化密切相关。
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3. **标题**: "Functional Analysis of Genetic Variants in GSTA1 and Their Impact on Drug Metabolism"
**作者**: McIlwain, C.C., et al.
**摘要**: 研究构建了多个GSTA1基因变体的重组蛋白，对比其酶活性和稳定性。发现某些单核苷酸多态性(SNPs)显著降低GSTA1对化疗药物(如环磷酰胺)的代谢能力，提示个体化用药的重要性。
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**备注**：以上文献信息为示例性概括，实际引用时需根据具体研究核实标题、作者及内容细节。建议通过PubMed或Web of Science以“GSTA1 recombinant protein”为关键词检索最新文献。
**Background of GSTA1 Recombinant Protein**
Glutathione S-transferase A1 (GSTA1) is a member of the glutathione S-transferase (GST) family, a group of phase II detoxification enzymes critical for cellular defense against oxidative stress and xenobiotic toxicity. GSTs catalyze the conjugation of glutathione (GSH) to electrophilic substrates, facilitating their metabolism and excretion. GSTA1. part of the GST Alpha class, is predominantly expressed in the liver, kidneys, and gastrointestinal tract, where it plays a central role in detoxifying carcinogens, environmental pollutants, and reactive oxygen species (ROS).
Recombinant GSTA1 protein is produced through genetic engineering techniques, often using bacterial (e.g., *E. coli*) or mammalian expression systems. This engineered protein retains the enzymatic activity of native GSTA1. making it a valuable tool for studying drug metabolism, oxidative stress responses, and chemical carcinogenesis. Its applications span *in vitro* assays to investigate substrate specificity, enzyme kinetics, and interactions with therapeutic agents or toxins.
In research, GSTA1 recombinant protein is also utilized to explore its role in diseases linked to detoxification deficits, such as cancer, neurodegenerative disorders, and drug-resistant phenotypes. Genetic polymorphisms in *GSTA1* have been associated with individual variations in drug efficacy and toxicity, highlighting its clinical relevance. Additionally, GSTA1’s ability to bind hydrophobic molecules has led to its use as a fusion tag for protein purification (GST-tag system), though this application typically employs GST from other isoforms (e.g., GST-tag derived from *Schistosoma japonicum*).
Structural studies of recombinant GSTA1 provide insights into its dimeric conformation, active-site architecture, and mechanisms of catalysis, aiding the design of inhibitors or modulators to target GST-related pathologies. Overall, GSTA1 recombinant protein serves as a cornerstone in biochemical, pharmacological, and toxicological research, bridging molecular mechanisms to therapeutic innovation.
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