| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MGEA5 |
| Uniprot No | O60502 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-916aa |
| 氨基酸序列 | MVQKESQATLEERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKASVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPTTLTKEEEKKQPDEEPMDMVVEKQEETDHKNDNQILSEIVEAKMAEELKPMDTDKESIAESKSPEMSMQEDCISDIAPMQTDEQTNKEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCGLVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGLPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL |
| 预测分子量 | 102,9 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MGEA5(O-GlcNAcase)重组蛋白的参考文献示例，内容基于相关领域的研究方向整理而成：
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1. **标题**：*"Expression and Characterization of Recombinant Human O-GlcNAcase in Escherichia coli"*
**作者**：Macauley, M.S., Whitworth, G.E., Vocadlo, D.J.
**摘要**：该研究描述了人源O-GlcNAcase(MGEA5)在大肠杆菌中的重组表达与纯化方法，通过亲和层析技术获得高纯度酶，并验证其水解O-GlcNAc修饰的活性，为后续酶学研究和抑制剂开发奠定基础。
2. **标题**：*"Structural Insights into the Catalytic Mechanism of Human O-GlcNAcase Using Crystallography"*
**作者**：Dennis, R.J., Taylor, E.J., Macauley, M.S.
**摘要**：通过X射线晶体学解析了重组MGEA5蛋白的三维结构，揭示了其底物结合域和催化机制，为设计靶向O-GlcNAcase的抑制剂提供了结构基础。
3. **标题**：*"Functional Analysis of O-GlcNAcase Isoforms in Cellular Models via Recombinant Expression"*
**作者**：Kim, E.J., Hanover, J.A.
**摘要**：研究利用哺乳动物细胞系统重组表达MGEA5的不同剪接变体，发现其在亚细胞定位和底物特异性上的差异，提示不同异构体在代谢调控中的独特作用。
4. **标题**：*"Development of a High-Throughput Screening Assay for O-GlcNAcase Activity Using Recombinant Enzyme"*
**作者**：Yuzwa, S.A., Vocadlo, D.J.
**摘要**：基于重组MGEA5蛋白建立了高通量荧光底物检测法，用于快速筛选酶活性调节剂，为糖尿病和神经退行性疾病的药物研发提供工具。
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**说明**：上述文献为示例性整理，实际引用时需查询具体数据库(如PubMed、Web of Science)获取真实文献的完整信息。核心研究方向包括重组蛋白表达、结构功能分析及酶学应用，可结合关键词“MGEA5”、“O-GlcNAcase”、“recombinant expression”进一步检索。
**Background of MGEA5 Recombinant Protein**
MGEA5 (Meningioma Expressed Antigen 5), also known as O-GlcNAcase (OGA), is a critical enzyme involved in the dynamic post-translational modification of proteins via the removal of β-N-acetylglucosamine (O-GlcNAc) residues. This reversible modification, termed O-GlcNAcylation, competes with phosphorylation to regulate diverse cellular processes, including transcription, signal transduction, and stress response. Dysregulation of O-GlcNAc cycling has been implicated in metabolic disorders (e.g., diabetes), neurodegenerative diseases (e.g., Alzheimer’s disease), and cancer, positioning MGEA5 as a therapeutic target.
Structurally, MGEA5 comprises a catalytic hydrolase domain and a C-terminal histone acetyltransferase-like domain, though its full functional mechanisms remain under investigation. Recombinant MGEA5 protein, typically produced in bacterial or eukaryotic expression systems, enables in vitro studies to dissect its enzymatic activity, substrate specificity, and interactions with inhibitors. For instance, Thiamet-G, a potent MGEA5 inhibitor, was developed using recombinant protein assays, highlighting its utility in drug discovery.
In neurodegenerative research, MGEA5 is linked to tau protein pathology, where aberrant O-GlcNAcylation may contribute to tau aggregation. In cancer, elevated MGEA5 expression correlates with tumor progression, possibly through metabolic reprogramming. The recombinant protein also aids structural studies, such as X-ray crystallography, to elucidate active-site architecture and guide inhibitor design.
Despite progress, challenges persist in understanding MGEA5’s dual enzymatic domains and tissue-specific regulation. Recombinant MGEA5 remains a vital tool for unraveling its biological roles and advancing therapeutic strategies targeting O-GlcNAc homeostasis.
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