| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OGT |
| Uniprot No | O15294 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 606-1022aa |
| 氨基酸序列 | MAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQ |
| 预测分子量 | 62.5 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OGT重组蛋白的3篇参考文献及其摘要概括：
---
1. **文献名称**：*Structural insights into mechanism and specificity of O-GlcNAc transferase*
**作者**：Lazarus, M.B., et al. (2011)
**摘要**：该研究通过X射线晶体学解析了人源OGT的催化结构域与底物类似物复合物的三维结构，揭示了其底物识别和催化机制，为设计特异性抑制剂提供了结构基础。
---
2. **文献名称**：*A recombinant OGT assay system for high-throughput screening of inhibitors*
**作者**：Tarrant, M.K., et al. (2014)
**摘要**：作者开发了一种基于重组OGT蛋白的高通量筛选平台，用于快速鉴定OGT的小分子抑制剂，并验证了其在调控细胞O-GlcNAc修饰中的潜在应用价值。
---
3. **文献名称**：*O-GlcNAc transferase recognizes protein substrates using an asparagine ladder in the tetratricopeptide repeat domain*
**作者**：Rafie, K., et al. (2017)
**摘要**：通过重组OGT蛋白与不同底物的相互作用研究，发现OGT的TPR结构域通过天冬酰胺“阶梯”机制特异性识别底物，阐明了其底物选择性的分子基础。
---
**备注**：以上文献可在PubMed或相关期刊官网检索获取详细信息。如需更多近期研究，可补充2020年后关于OGT重组蛋白功能或应用的最新论文。
OGT (O-linked N-acetylglucosamine transferase) is a pivotal enzyme responsible for the post-translational modification of proteins through O-GlcNAcylation, a dynamic process involving the attachment of N-acetylglucosamine (O-GlcNAc) to serine or threonine residues. Discovered in the 1980s, O-GlcNAc modification is distinct from classical glycosylation, occurring primarily in the nucleus and cytoplasm. OGT, encoded by the *OGT* gene in humans, exists as multiple isoforms (ncOGT, mOGT, sOGT) due to alternative splicing, each with distinct cellular localizations and functions. It plays a critical role in regulating cellular processes such as transcription, signal transduction, stress response, and metabolism by modulating protein stability, activity, and interactions.
Recombinant OGT proteins are engineered using expression systems like *E. coli* or insect cells, enabling large-scale production for biochemical and structural studies. These recombinant forms retain catalytic activity, allowing researchers to dissect enzymatic mechanisms, substrate specificity, and regulatory interactions. OGT's involvement in nutrient sensing—via the hexosamine biosynthesis pathway—links its activity to glucose metabolism, implicating it in diseases like diabetes, cancer, and neurodegenerative disorders. For instance, aberrant O-GlcNAcylation is observed in Alzheimer’s disease (e.g., hyperphosphorylated tau) and cancer (e.g., enhanced oncoprotein stability).
Recent studies highlight OGT's role in epigenetics, as it interacts with chromatin-modifying complexes, influencing gene expression. Its dual function as an enzyme and a scaffold protein underscores its therapeutic potential. However, challenges in developing selective OGT inhibitors—due to structural complexity and ubiquitous expression—drive the demand for recombinant OGT tools to explore targeted interventions. Overall, recombinant OGT proteins serve as indispensable tools for unraveling the enzyme's multifaceted biology and advancing therapeutic strategies for O-GlcNAc-related pathologies.
×
