| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLO2 |
| Uniprot No | Q16775 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-260aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMKVEVLPALTDNYMYLVIDDETKEAA IVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVY GGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSE PPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYT INNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMR VREKTVQQHAGETDPVTTMRAVRREKDQFKMPRD |
| 预测分子量 | 31 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篇关于GLO2(乙二醛酶II)重组蛋白的虚构参考文献示例(基于常见研究方向整理，实际文献需通过学术数据库查询)：
1. **《Expression and Functional Analysis of Recombinant Human GLO2 in E. coli》**
- 作者：Zhang, L. et al.
- 摘要：研究通过大肠杆菌系统成功表达并纯化重组人源GLO2蛋白，验证其酶活性及对甲基乙二醛(MG)的解毒功能，为后续疾病治疗研究提供基础。
2. **《Structural Insights into GLO2 Catalytic Mechanism via Crystallography》**
- 作者：Smith, J. & Kumar, R.
- 摘要：利用X射线晶体学解析重组GLO2蛋白的三维结构，阐明其底物结合位点及催化机制，揭示金属离子在酶活性中的关键作用。
3. **《Recombinant GLO2 Attenuates Oxidative Stress in Diabetic Mouse Models》**
- 作者：Chen, Y. et al.
- 摘要：在糖尿病小鼠模型中，注射重组GLO2蛋白显著降低氧化应激标志物水平，改善胰岛素抵抗，提示其潜在代谢疾病治疗价值。
注：以上为模拟示例，实际文献需通过PubMed、Google Scholar等平台以“GLO2 recombinant protein”“glyoxalase II”等关键词检索。
Glyoxalase 2 (GLO2), also known as hydroxyacylglutathione hydrolase, is a critical enzyme in the glyoxalase system, a metabolic pathway responsible for detoxifying methylglyoxal (MG), a highly reactive byproduct of glycolysis. MG accumulation is cytotoxic, contributing to oxidative stress, protein glycation, and DNA damage, which are implicated in aging, diabetes, neurodegenerative disorders, and cancer. The glyoxalase system comprises two enzymes: GLO1. which catalyzes the isomerization of MG into S-D-lactoylglutathione, and GLO2. which hydrolyzes this intermediate to yield non-toxic D-lactate and regenerate glutathione, a key cellular antioxidant.
Recombinant GLO2 proteins are engineered versions of the enzyme produced via genetic engineering in heterologous expression systems such as *E. coli*, yeast, or mammalian cell cultures. These systems enable large-scale production of purified, bioactive GLO2 for research and therapeutic applications. Recombinant technology allows for modifications like tagging (e.g., His-tag) to facilitate purification or tracking, or site-directed mutagenesis to study structure-function relationships. Structural studies using recombinant GLO2 have revealed its zinc-dependent metalloenzyme activity and conserved catalytic mechanisms across species.
Research on recombinant GLO2 has advanced understanding of its role in cellular redox homeostasis and disease pathogenesis. Dysregulation of GLO2 is linked to diabetic complications, Alzheimer’s disease, and cancer progression, making it a potential therapeutic target or biomarker. Recombinant proteins are also used to screen inhibitors or activators for drug development. Despite progress, challenges remain in optimizing enzyme stability, activity, and delivery for clinical applications. Overall, recombinant GLO2 serves as a vital tool for elucidating MG detoxification pathways and developing interventions against MG-associated pathologies.
×
