| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTT1 |
| Uniprot No | P30711 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-240aa |
| 氨基酸序列 | GLELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKYKVPDYWYPQDLQARARVDEYLAWQHTTLRRSCLRALWHKVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVAITELMHPVGAGCQVFEGRPKLATWRQRVEAAVGEDLFQEAHEVILKAKDFPPADPTIKQKLMPWVLAMIR |
| 预测分子量 | 34.1 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GSTT1重组蛋白的3-4条参考文献示例(注：文献为虚拟示例，实际引用需查证真实来源)：
1. **文献名称**：*Expression and Functional Characterization of Recombinant GSTT1 in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：报道了在大肠杆菌中成功表达GSTT1重组蛋白的方法，验证其谷胱甘肽结合活性及对特定环境毒素的代谢能力，为酶功能研究提供工具。
2. **文献名称**：*Structural Insights into GSTT1 Substrate Specificity by Mutagenesis Analysis*
**作者**：Johnson R, et al.
**摘要**：通过定点突变和X射线晶体学解析GSTT1重组蛋白的结构，揭示其底物结合口袋的关键氨基酸残基，解释不同人群基因多态性对酶活性的影响。
3. **文献名称**：*GSTT1 Null Genotype and Cancer Risk: Role of Recombinant Protein in Detoxification Studies*
**作者**：Chen L, et al.
**摘要**：利用GSTT1重组蛋白模型，证明其缺失型(null型)人群对致癌物代谢能力下降，体外实验验证其与DNA加合物形成的关联性。
4. **文献名称**：*Recombinant GSTT1 as a Tool for Drug Metabolism Screening*
**作者**：Brown K, et al.
**摘要**：开发基于GSTT1重组蛋白的高通量药物代谢检测体系，评估其参与化疗药物代谢的潜力，为个体化用药提供依据。
(注：以上为模拟内容，实际文献需通过PubMed/Google Scholar等平台检索确认。)
Glutathione S-transferase theta-1 (GSTT1) 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, including environmental toxins, carcinogens, and therapeutic drugs. This conjugation enhances the solubility of these compounds, facilitating their excretion and reducing cellular damage. GSTT1 is encoded by the GSTT1 gene, located on chromosome 22q11.23. and exhibits genetic polymorphism, with a common null allele (GSTT1*0) resulting in complete enzyme deficiency in approximately 10–20% of global populations. This polymorphism influences individual susceptibility to chemical toxicity, drug efficacy, and disease risk.
Recombinant GSTT1 protein is produced via heterologous expression systems, such as E. coli or mammalian cell lines (e.g., HEK293. CHO), enabling large-scale purification for functional studies. Structurally, GSTT1 adopts a typical GST fold, comprising an N-terminal thioredoxin-like domain for GSH binding and a C-terminal α-helical domain that contributes to substrate specificity. Unlike other GST isoforms, GSTT1 shows restricted substrate specificity, primarily metabolizing halogenated alkanes, ethylene oxide, and certain chemotherapeutic agents.
Research applications of recombinant GSTT1 include elucidating metabolic pathways, assessing drug–enzyme interactions, and modeling detoxification mechanisms in vitro. It is also used to study the impact of GSTT1 polymorphisms on enzyme activity and disease associations, particularly in cancer (e.g., colorectal, lung), neurodegenerative disorders, and environmental toxin exposure. Additionally, recombinant GSTT1 serves as a tool in high-throughput screening for inhibitors or activators to modulate detoxification capacity. Its role in cellular redox balance and apoptosis regulation further underscores its relevance in biomedical research, making it a critical reagent for understanding chemical biology and personalized medicine strategies.
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