| 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.
在生物科技领域，蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者，凭借自身卓越的研发实力，每年能成功研发 1000 多种全新蛋白，在重组蛋白领域不断突破。 在重组蛋白生产过程中，艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白，到具有特定催化功能的酶、参与信号传导的激酶，再到用于免疫研究的病毒抗原，艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统，昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势，能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求，从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品，更是从源头到终端的一站式解决方案。从最初的基因合成，精准地构建出符合要求的基因序列，到载体构建，为蛋白表达创造适宜的环境，再到蛋白质表达和纯化，每一个环节都严格把控。我们充分尊重客户的个性化需求，在表达 / 纯化标签的选择、表达宿主的确定等方面，为客户量身定制专属方案。 同时，艾普蒂还配备了多种纯化体系，能够应对不同特性蛋白的纯化需求。这种灵活性和专业性，极大地提高了蛋白表达和纯化的成功率，让客户的研究项目得以顺利推进，在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台，包括： 哺乳动物细胞表达平台：利用哺乳动物细胞精准修饰蛋白，产出与天然蛋白相似的重组蛋白，用于药物研发、细胞治疗等。 杂交瘤开发平台：通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株，优化后的技术让抗体亲和力与特异性更高，应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台：FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞；Beacon® 基于微流控技术，单细胞水平捕获、分析 B 细胞，挖掘抗体多样性，缩短开发周期。 凭借这些平台，艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务，推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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