| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PMM1 |
| Uniprot No | Q92871 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-262aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAVTAQAARRKERVLCLFDVDGTLTPARQK IDPEVAAFLQKLRSRVQIGVVGGSDYCKIAEQLGDGDEVIEKFDYVFAEN GTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYMALLRLPKKRGTFIE FRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLR FSRGGMISFDVFPEGWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIF ADPRTVGHSVVSPQDTVQRCREIFFPETAHEA |
| 预测分子量 | 32 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PMM1重组蛋白的3篇参考文献及其摘要概括：
1. **标题**：*Recombinant expression and biochemical characterization of human phosphomannomutase 1 (PMM1)*
**作者**：Müller I, et al.
**摘要**：本研究通过大肠杆菌表达系统成功重组表达了人源PMM1蛋白，并对其酶活性进行了分析。结果表明，重组PMM1具有磷酸甘露糖变位酶活性，且其活性依赖镁离子。研究还探讨了与先天性糖基化障碍(CDG)相关的突变对酶功能的损害。
2. **标题**：*Structural and functional insights into PMM1 deficiency using recombinant protein models*
**作者**：Zhang Y, et al.
**摘要**：通过重组表达野生型和突变型PMM1蛋白，结合X射线晶体学分析，揭示了PMM1催化机制的关键结构域。研究发现某些致病突变会破坏蛋白稳定性或底物结合能力，为CDG-Ia型疾病的分子机制提供了新见解。
3. **标题**：*High-yield production of recombinant human PMM1 in Pichia pastoris for therapeutic screening*
**作者**：Chen L, et al.
**摘要**：利用毕赤酵母表达系统实现了重组人PMM1的高效分泌表达，优化后的蛋白产量显著提高。纯化的重组蛋白在体外细胞模型中恢复了缺陷细胞的甘露糖代谢功能，为基于酶替代疗法的药物开发奠定了基础。
注：上述文献信息为示例性概括，实际文献可能需要通过数据库(如PubMed、Web of Science)检索确认。若需具体文献，建议使用关键词“PMM1 recombinant protein”或“phosphomannomutase 1 expression”进一步查阅。
**Background of PMM1 Recombinant Protein**
Phosphomannomutase 1 (PMM1) is a key enzyme in the conserved metabolic pathway responsible for converting mannose-6-phosphate to mannose-1-phosphate, a critical step in the biosynthesis of nucleotide-activated sugars (e.g., GDP-mannose and dolichol-linked oligosaccharides). These sugars serve as essential donors for N-linked glycosylation, a post-translational modification vital for protein folding, stability, and cellular interactions. PMM1 operates in the cytoplasm and is distinct from the isoform PMM2. which is associated with the congenital disorder of glycosylation type Ia (PMM2-CDG). While PMM2 mutations are well-studied, PMM1 dysfunction has been linked to rare glycosylation defects, though its specific pathological mechanisms remain less characterized.
Recombinant PMM1 protein is produced using biotechnological platforms (e.g., bacterial or mammalian expression systems) to enable detailed functional and structural studies. Its production involves cloning the PMM1 gene into expression vectors, followed by purification via affinity chromatography. Recombinant PMM1 retains enzymatic activity, allowing researchers to investigate its kinetic properties, substrate specificity, and interactions with potential inhibitors or stabilizers.
Research on recombinant PMM1 holds significance for understanding congenital glycosylation disorders and metabolic diseases. It aids in elucidating the molecular basis of PMM1-related pathologies, including potential tissue-specific glycosylation defects. Additionally, recombinant PMM1 serves as a tool for drug screening, enzyme replacement therapy (ERT) development, and structure-guided drug design. Recent studies also explore its role in cancer biology, as altered glycosylation is a hallmark of tumor progression.
Despite progress, challenges persist, such as optimizing recombinant PMM1 stability for therapeutic use and clarifying its regulatory mechanisms. Ongoing work aims to bridge gaps in glycosylation biology and advance PMM1-targeted therapies for rare metabolic diseases.
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