| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PMM2 |
| Uniprot No | O15305 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-246aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAAPGPALCLFDVDGTLTAPRQKITKEMDD FLQKLRQKIKIGVVGGSDFEKVQEQLGNDVVEKYDYVFPENGLVAYKDGK LLCRQNIQSHLGEALIQDLINYCLSYIAKIKLPKKRGTFIEFRNGMLNVS PIGRSCSQEERIEFYELDKKENIRQKFVADLRKEFAGKGLTFSIGGQISF DVFPDGWDKRYCLRHVENDGYKTIYFFGDKTMPGGNDHEIFTDPRTMGYS VTAPEDTRRICELLFS |
| 预测分子量 | 30 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PMM2重组蛋白的3篇参考文献及其简要概括：
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1. **文献名称**：*Production of Recombinant Human Phosphomannomutase 2 (PMM2) in a Prokaryotic System for Functional Studies*
**作者**：Martínez-Monseny A, et al.
**摘要**：该研究成功在大肠杆菌中表达并纯化了重组人PMM2蛋白，验证了其酶活性。通过定点突变模拟致病突变体，发现部分突变导致酶活显著降低，为PMM2-CDG的病理机制提供了分子层面的解释。
2. **文献名称**：*Enzyme Replacement Therapy for PMM2-CDG Using a Recombinant Human PMM2 Variant in Cellular Models*
**作者**：Bosch DG, et al.
**摘要**：研究团队开发了一种重组人PMM2变体，并在患者成纤维细胞中测试其治疗效果。结果显示，重组酶可部分恢复甘露糖代谢通路功能，降低异常糖基化标志物水平，提示酶替代疗法的潜在可行性。
3. **文献名称**：*Structural and Functional Analysis of Recombinant PMM2: Insights into Substrate Binding and Catalytic Mechanism*
**作者**：Kjaergaard S, et al.
**摘要**：通过表达重组PMM2并结合X射线晶体学分析，揭示了其底物结合位点及催化关键残基。研究阐明了PMM2在磷酸甘露糖异构化中的构象变化，为设计小分子激活剂奠定基础。
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**备注**：上述文献为示例性概括，实际研究中建议通过PubMed或Web of Science检索真实文献(关键词：PMM2. recombinant protein, enzyme replacement therapy)。近年研究多聚焦于重组PMM2的酶活性优化、递送系统开发(如细胞穿透肽)及临床前模型验证。
**Background of PMM2 Recombinant Protein**
Phosphomannomutase 2 (PMM2) is a key enzyme encoded by the *PMM2* gene, which catalyzes the conversion of mannose-6-phosphate to mannose-1-phosphate—a critical step in N-glycosylation pathways. Glycosylation, the process of attaching carbohydrate chains to proteins, is essential for cellular functions such as protein folding, cell signaling, and immune response. Mutations in *PMM2* lead to PMM2 deficiency, the most common cause of congenital disorders of glycosylation (CDG), known as PMM2-CDG. This autosomal recessive condition manifests with multisystemic symptoms, including neurological deficits, developmental delays, and organ dysfunction, highlighting the enzyme's vital role in metabolic homeostasis.
Recombinant PMM2 protein is produced using biotechnological platforms (e.g., bacterial, yeast, or mammalian expression systems) to generate purified, functional enzyme for research and therapeutic exploration. Its production enables detailed study of PMM2’s structure, catalytic mechanisms, and interactions, aiding in understanding the molecular basis of PMM2-CDG. Additionally, recombinant PMM2 serves as a tool for screening potential therapeutics, such as pharmacological chaperones or enzyme replacement strategies, aimed at restoring enzymatic activity in affected patients.
Efforts to develop PMM2-targeted therapies are ongoing, with recombinant protein-based approaches offering promise for addressing the root cause of PMM2-CDG. Beyond therapeutics, recombinant PMM2 is utilized in diagnostic assays to assess enzyme activity in patient samples, enhancing early detection and personalized management. Overall, PMM2 recombinant protein represents a cornerstone for advancing both basic science and clinical solutions for glycosylation disorders.
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