| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSS |
| Uniprot No | P48637 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-474aa |
| 氨基酸序列 | ATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF TLFPSLVPSA LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT ARLFDIHKQV LKEGIAQTVF LGLNRSDYMF QRSADGSPAL KQIEINTISA SFGGLASRTP AVHRHVLSVL SKTKEAGKIL SNNPSKGLAL GIAKAWELYG SPNALVLLIA QEKERNIFDQ RAIENELLAR NIHVIRRTFE DISEKGSLDQ DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA IAEALAAPSR FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK IEPEPFENCL LRPGSPARVV QCISELGIFG VYVRQEKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV |
| 预测分子量 | 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3篇与GSS(谷胱甘肽合成酶)重组蛋白相关的模拟参考文献示例(注：文献信息为虚构，仅作格式参考)：
---
1. **文献名称**：*High-Yield Expression and Purification of Recombinant Human Glutathione Synthetase in E. coli*
**作者**：Chen L, Wang Y, et al.
**摘要**：本研究构建了人源GSS基因的重组表达载体，通过大肠杆菌表达系统优化实现了可溶性GSS蛋白的高效表达，并利用亲和层析技术获得高纯度蛋白，为酶学机制研究提供材料基础。
---
2. **文献名称**：*Structural Insights into the Catalytic Mechanism of Recombinant GSS via Crystallography*
**作者**：Smith J, Tanaka K, et al.
**摘要**：通过X射线晶体学解析了重组GSS蛋白的三维结构，揭示了其底物结合位点及催化活性中心的关键氨基酸残基，为开发靶向GSS的抗氧化药物提供结构依据。
---
3. **文献名称**：*Therapeutic Potential of Recombinant GSS in a Mouse Model of Oxidative Stress-Induced Neurodegeneration*
**作者**：Gupta R, Lee S, et al.
**摘要**：在氧化应激诱导的神经退行性疾病小鼠模型中，腹腔注射重组GSS蛋白显著提高了脑组织谷胱甘肽水平，减轻神经元损伤，提示其作为神经保护剂的潜力。
---
(注：实际文献需通过PubMed/Google Scholar等平台以“recombinant glutathione synthetase”或“GSS protein expression”为关键词检索。)
**Background of GSS Recombinant Protein**
Glutathione synthetase (GSS) is a critical enzyme in the biosynthesis of glutathione (GSH), a tripeptide antioxidant essential for cellular defense against oxidative stress, detoxification, and immune regulation. GSS catalyzes the final step of GSH synthesis, combining γ-glutamylcysteine with glycine to form GSH. Deficiencies in GSS activity, caused by genetic mutations or environmental factors, are linked to metabolic disorders, hemolytic anemia, and neurological dysfunction, underscoring its physiological importance.
The development of recombinant GSS protein leverages genetic engineering to express and purify the enzyme in heterologous systems, such as *E. coli*, yeast, or mammalian cell cultures (e.g., CHO cells). This approach ensures high purity, scalability, and consistent activity, overcoming limitations of isolating the enzyme from native tissues. Recombinant GSS serves as a vital tool for studying enzymatic mechanisms, substrate interactions, and structural features via X-ray crystallography or cryo-EM, aiding in the design of modulators for therapeutic or industrial use.
Applications of recombinant GSS span biomedical research and biotechnology. It is used to model GSS deficiency disorders, screen potential therapeutics, and produce GSH for pharmaceutical or cosmetic industries. In drug development, recombinant GSS is explored as a protein replacement therapy or adjuvant in antioxidant treatments. Additionally, engineered GSS variants with enhanced stability or catalytic efficiency are being investigated for industrial biocatalysis.
Despite progress, challenges remain in optimizing expression yields, ensuring post-translational modifications in prokaryotic systems, and understanding tissue-specific regulation of GSS. Ongoing research aims to address these gaps, positioning recombinant GSS as a cornerstone in advancing both basic science and translational applications related to oxidative stress and metabolic health.
×
