| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTa5 |
| Uniprot No | Q7RTV2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-222aa |
| 氨基酸序列 | AEKPKLHYS NARGSMESIR WLLAAAGVEL EEKFLESAED LDKLRNDGSL LFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDMKERA LIDMYTEGIV DLTEMILLLL ICQPEERDAK TALVKEKIKN RYFPAFEKVL KSHRQDYLVG NKLSWADIHL VELFYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP GSQRKPPMDE KSLEEARKIF RF |
| 预测分子量 | 25,7 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GSTa5重组蛋白的虚构参考文献示例(内容为模拟生成，非真实文献)：
1. **文献名称**：*Expression and purification of recombinant GSTa5 in E. coli for enzymatic studies*
**作者**：Chen L, Wang Y, et al.
**摘要**：本研究成功构建了GSTa5重组蛋白的原核表达系统，通过优化诱导条件提高蛋白可溶性表达，并利用谷胱甘肽亲和层析纯化获得高纯度蛋白，验证其谷胱甘肽结合活性。
2. **文献名称**：*Structural characterization of GSTa5 reveals substrate specificity determinants*
**作者**：Zhang R, Liu X, et al.
**摘要**：通过X射线晶体学解析GSTa5的三维结构，结合分子对接实验阐明其底物结合口袋的关键氨基酸残基，揭示了GSTa5对特定亲电底物的催化机制。
3. **文献名称**：*Functional analysis of GSTa5 in drug metabolism using CRISPR/Cas9 knockout models*
**作者**：Kim J, Patel S, et al.
**摘要**：利用基因编辑技术构建GSTa5敲除细胞模型，证明GSTa5在药物代谢解毒中的重要作用，重组蛋白体外实验进一步验证其对化疗药物的代谢活性。
4. **文献名称**：*GSTa5 recombinant protein as a tool for detoxification pathway studies in hepatocytes*
**作者**：Gupta A, Fernández-Molina C, et al.
**摘要**：将重组GSTa5导入肝细胞，发现其显著增强细胞对氧化应激的抵抗能力，提示其在肝脏疾病治疗中的潜在应用价值。
(注：以上文献信息均为示例性虚构内容，实际研究中请通过学术数据库检索真实文献。)
GSTα5 (Glutathione S-transferase alpha 5) is a member of the glutathione S-transferase (GST) superfamily, a group of enzymes critical for cellular detoxification and antioxidant defense. These enzymes catalyze the conjugation of glutathione (GSH) to electrophilic substrates, facilitating the neutralization and excretion of xenobiotics, environmental toxins, and reactive oxygen species. The GSTα subclass, including GSTα5. is predominantly expressed in mammalian liver and plays a key role in phase II drug metabolism. GSTα5 specifically has garnered attention due to its unique substrate specificity and regulatory mechanisms compared to other GST isoforms.
Recombinant GSTα5 protein is engineered through genetic cloning and expression systems (e.g., *E. coli*, mammalian cells) to study its structural and functional properties. Its recombinant form retains enzymatic activity, enabling researchers to explore its interactions with therapeutic drugs, carcinogens, and endogenous metabolites. The protein’s structure—characterized by a conserved N-terminal glutathione-binding domain and a C-terminal substrate-binding region—provides insights into catalytic mechanisms and ligand specificity.
Research on recombinant GSTα5 has implications for understanding drug resistance in cancers, as GST overexpression is linked to chemotherapeutic detoxification. Additionally, it serves as a tool in toxicology to assess chemical-induced oxidative stress responses. Beyond biomedical applications, GSTα5 recombinant protein is utilized in biotechnology as a fusion tag for protein purification (GST-tag system), leveraging its affinity for glutathione-coated matrices. Ongoing studies aim to elucidate its role in metabolic diseases, inflammation, and personalized medicine, highlighting its versatility as both a biological target and a practical research reagent.
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