| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLP1 |
| Uniprot No | P60201 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-277aa |
| 氨基酸序列 | GLLECCARCLVGAPFASLVATGLCFFGVALFCGCGHEALTGTEKLIETYF SKNYQDYEYLINVIHAFQYVIYGTASFFFLYGALLLAEGFYTTGAVRQIF GDYKTTICGKGLSATVTGGQKGRGSRGQHQAHSLERVCHCLGKWLGHPDK FVGITYALTVVWLLVFACSAVPVYIYFNTWTTCQSIAFPSKTSASIGSLC ADARMYGVLPWNAFPGKVCGSNLLSICKTAEFQMTFHLFIAAFVGAAATL VSLLTFMIAATYNFAVLKLMGRGTKF |
| 预测分子量 | 36 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PLP1重组蛋白的3篇代表性文献(内容基于已有研究领域知识整理，具体细节需以实际文献为准)：
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1. **文献名称**：*"Expression and purification of recombinant human PLP1 in Escherichia coli for structural studies"*
**作者**：Thiessen, G., & Yamamoto, S.
**摘要**：本研究报道了通过大肠杆菌表达系统高效表达人源PLP1重组蛋白的优化策略，并利用亲和层析技术纯化获得高纯度蛋白。通过圆二色谱和X射线晶体学分析，揭示了PLP1的跨膜结构域特征，为研究其与髓鞘稳定性相关的分子机制提供基础。
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2. **文献名称**：*"Functional characterization of PLP1 mutations in a mammalian cell model using recombinant protein expression"*
**作者**：Jones, R.L., Simons, M., & Werner, H.B.
**摘要**：作者在哺乳动物细胞(HEK293)中表达了野生型及突变型PLP1重组蛋白，结合免疫荧光和蛋白质印迹技术，揭示了PLP1异常折叠与内质网应激的相关性。该研究为佩梅氏病的病理机制提供了分子层面证据。
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3. **文献名称**：*"Recombinant PLP1 as an antigenic target for autoantibody detection in demyelinating disorders"*
**作者**：Greer, J.M., & Lees, M.B.
**摘要**：研究利用昆虫细胞(杆状病毒系统)表达重组PLP1蛋白，并验证其作为抗原在实验性自身免疫性脑脊髓炎(EAE)模型中的应用。结果表明重组PLP1可特异性识别患者血清中的自身抗体，为多发性硬化症的诊断提供了潜在工具。
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**注**：以上文献信息为模拟示例，实际研究中请通过PubMed、Web of Science等数据库检索具体文献。
PLP1 (Proteolipid Protein 1) is a critical transmembrane protein predominantly expressed in the central nervous system (CNS), where it constitutes ~50% of myelin sheath content. As a structural component of myelin, PLP1 maintains axon insulation and facilitates efficient nerve impulse conduction. The human PLP1 gene, located on the X chromosome (Xq22.2), encodes two major splice variants: the full-length PLP1 (276 amino acids) and its shorter isoform DM20. Both isoforms feature four transmembrane domains but differ in a hydrophilic intracellular loop region, influencing their functional roles in myelination and oligodendrocyte development.
Mutations in PLP1 are linked to Pelizaeus-Merzbacher disease (PMD), a rare X-linked leukodystrophy characterized by hypomyelination, neurodevelopmental deficits, and motor dysfunction. Over 200 PLP1 mutations (duplications, point mutations, deletions) have been identified, with gene duplication accounting for 60-70% of PMD cases. These genetic alterations disrupt myelin compaction, oligodendrocyte survival, and intracellular trafficking, making PLP1 a key focus in demyelination research.
Recombinant PLP1 protein, typically produced in Escherichia coli or mammalian expression systems, enables mechanistic studies of myelination and PMD pathology. Researchers utilize it to investigate protein-membrane interactions, mutation-induced conformational changes, and potential therapeutic interventions. Its applications extend to antibody generation for diagnostic assays, drug screening platforms, and biomimetic myelin models. However, challenges persist in replicating native post-translational modifications (e.g., palmitoylation) critical for PLP1's membrane association and function. Current efforts focus on optimizing eukaryotic expression systems to produce biologically active PLP1 for translational studies.
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