| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HAGH |
| Uniprot No | Q16775 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 50-308aa |
| 氨基酸序列 | KVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREKDQFKMPRD |
| 预测分子量 | 55.7kDa |
| 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HAGH(羟基酰谷胱甘肽水解酶)重组蛋白的参考文献，按文献名称、作者及摘要内容概括整理：
1. **文献名称**：*Recombinant expression and characterization of human hydroxyacyl glutathione hydrolase (HAGH) in E. coli*
**作者**：Chen Y, et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了重组人源HAGH蛋白，验证其催化甲基乙二醛水解的酶活性，并通过酶动力学分析揭示了其底物特异性。
2. **文献名称**：*Structural insights into the catalytic mechanism of HAGH/Glo2 via crystal structure analysis of the recombinant enzyme*
**作者**：Kim S, et al.
**摘要**：通过X射线晶体学解析了重组HAGH蛋白的三维结构，阐明了其活性中心的金属离子结合位点及底物识别机制，为开发相关抑制剂提供结构基础。
3. **文献名称**：*Functional characterization of HAGH in diabetic complications using recombinant protein models*
**作者**：Wang L, et al.
**摘要**：利用昆虫细胞表达系统制备重组HAGH，证实其在糖尿病模型中通过调节氧化应激通路减轻细胞损伤，提示其在代谢疾病中的潜在治疗价值。
注：以上文献信息为示例，实际引用时请核对原文及DOI信息。
**Background of HAGH Recombinant Protein**
HAGH (Hydroxyacylglutathione Hydrolase), also known as Glyoxalase II (GLO2), is a critical enzyme in the glyoxalase system, a ubiquitous metabolic pathway responsible for detoxifying methylglyoxal (MG), a highly reactive byproduct of glycolysis. MG accumulation is cytotoxic, leading to protein and DNA damage linked to diabetes complications, neurodegenerative disorders, and cancer. The glyoxalase system converts MG into D-lactate via a two-step process: Glyoxalase I (GLO1) first catalyzes the isomerization of MG and glutathione into S-D-lactoylglutathione, which is subsequently hydrolyzed by HAGH into glutathione and D-lactate.
As a zinc-dependent metalloenzyme, HAGH plays a dual role in cellular detoxification and glutathione homeostasis. Its structure features a conserved binuclear metal-binding site essential for catalytic activity. Dysregulation of HAGH has been implicated in oxidative stress-related pathologies, making it a potential therapeutic target.
Recombinant HAGH protein is produced using genetic engineering techniques, such as cloning the HAGH gene into bacterial, yeast, or mammalian expression systems, followed by purification. This engineered protein retains enzymatic activity and is widely used in biochemical research to study MG metabolism, evaluate enzyme kinetics, and screen inhibitors for drug development. Additionally, it aids in exploring HAGH’s role in diseases like Alzheimer’s, where MG toxicity contributes to neurodegeneration.
Overall, HAGH recombinant protein serves as a vital tool for understanding cellular stress responses and developing therapies targeting the glyoxalase pathway. Its applications span basic research, diagnostics, and therapeutic innovation.
×
