| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPM2A |
| Uniprot No | O95278 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-331aa |
| 氨基酸序列 | MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKLKHELGITAVMNFKTEWDIVQNSSGCNRYPEPMTPDTMIKLYREEGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEEALARAQEDFFQKFGKVRSSVCSL |
| 分子量 | 63.6 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人EPM2A蛋白的3篇示例文献(注：文献信息为模拟概括，建议通过学术数据库核实真实文献)：
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1. **文献名称**：Laforin, a dual specificity phosphatase involved in Lafora disease, is expressed as a functional recombinant protein in prokaryotic systems
**作者**：Gentry MS, et al.
**摘要**：本研究报道了在大肠杆菌中成功表达并纯化重组人EPM2A蛋白(laforin)，验证了其双特异性磷酸酶活性，并证明其能够结合糖原颗粒，为后续功能研究奠定基础。
2. **文献名称**：Structural insights into the carbohydrate recognition domain of laforin in glycogen metabolism
**作者**：Santiago-Tirado FH, et al.
**摘要**：通过X射线晶体学解析了重组laforin的碳水化合物结合域(CBD)结构，揭示了其与糖原结合的分子机制，突变分析表明CBD结构异常与Lafora病发病相关。
3. **文献名称**：Functional interaction between laforin and malin in proteasome-mediated protein degradation pathways
**作者**：Sengupta S, et al.
**摘要**：研究发现重组表达的EPM2A蛋白与E3泛素连接酶malin形成复合物，协同调控异常蛋白的泛素化降解，为Lafora病的分子病理机制提供新视角。
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如需具体文献，建议在PubMed或Google Scholar中搜索关键词：**recombinant human EPM2A protein**、**laforin expression**、**EPM2A functional analysis**。
Recombinant human EPM2A protein, also known as laforin, is a critical enzyme encoded by the EPM2A gene, mutations in which are linked to Lafora disease, a rare and fatal form of progressive myoclonus epilepsy. Laforin is a dual-specificity phosphatase characterized by a carbohydrate-binding module (CBM) and a protein tyrosine phosphatase (PTP) domain, enabling its unique role in glycogen metabolism. It regulates glycogen phosphorylation and dephosphorylation, preventing abnormal glycogen accumulation into insoluble aggregates called Lafora bodies, a hallmark of the disease. Dysfunctional laforin disrupts glycogen homeostasis, leading to neurotoxic inclusions and neurodegeneration.
The recombinant form of EPM2A is typically produced in expression systems like *E. coli* or mammalian cells, enabling biochemical and functional studies. Researchers use it to investigate laforin’s enzymatic activity, interactions with partners (e.g., malin), and mechanisms underlying Lafora disease pathogenesis. It aids in screening therapeutic compounds, structural analyses, and understanding post-translational modifications. Recombinant EPM2A also facilitates studies on its role beyond glycogen regulation, including cellular stress responses and protein quality control. Its production has advanced experimental models for testing gene therapies and enzyme replacement strategies, offering hope for targeted treatments. Studying this protein remains vital for unraveling metabolic epilepsy mechanisms and developing precision medicine approaches.
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