| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | plp |
| 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 | GLLECCARCLVGAPFASLVATGLCFFGVALFCGCGHEALTGTEKLIETYFSKNYQDYEYLINVIHAFQYVIYGTASFFFLYGALLLAEGFYTTGAVRQIFGDYKTTICGKGLSATVTGGQKGRGSRGQHQAHSLERVCHCLGKWLGHPDKFVGITYALTVVWLLVFACSAVPVYIYFNTWTTCQSIAFPSKTSASIGSLCADARMYGVLPWNAFPGKVCGSNLLSICKTAEFQMTFHLFIAAFVGAAATLVSLLTFMIAATYNFAVLKLMGRGTKF |
| 预测分子量 | 30,0 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PLP重组蛋白的3篇示例参考文献(内容为虚构示例，供参考格式)：
1. **文献名称**: "High-yield expression and purification of recombinant human PLP in E. coli for immunological studies"
**作者**: Zhang et al.
**摘要**: 研究报道了通过大肠杆菌表达系统高效生产重组人源PLP蛋白的方法，优化了纯化工艺，并验证其在多发性硬化症动物模型中诱导自身免疫反应的抗原活性。
2. **文献名称**: "Structural characterization of recombinant PLP using cryo-EM reveals its role in myelin membrane assembly"
**作者**: Müller & Schmidt
**摘要**: 通过冷冻电镜技术解析了重组PLP蛋白的三维结构，揭示了其疏水结构域在髓鞘脂质双层组装中的关键作用，为脱髓鞘疾病的机制研究提供依据。
3. **文献名称**: "Recombinant PLP1 fusion protein as a therapeutic vaccine in experimental autoimmune encephalomyelitis"
**作者**: Gupta et al.
**摘要**: 开发了一种PLP1与免疫调节因子的重组融合蛋白，证明其在小鼠EAE模型中能有效抑制炎症反应并减轻神经功能损伤，提示潜在临床治疗价值。
(注：若需真实文献，建议通过PubMed/Google Scholar检索关键词“recombinant PLP protein”或结合具体研究领域筛选。)
**Background of PLP Recombinant Protein**
Proteolipid protein (PLP), a major component of myelin in the central nervous system (CNS), plays a critical role in maintaining the structural integrity and functional stability of myelinated axons. As a transmembrane protein encoded by the *PLP1* gene, it constitutes approximately 50% of myelin protein content and is essential for compact myelin formation. PLP’s hydrophobic nature and complex membrane-spanning structure have historically posed challenges for its isolation and characterization.
Recombinant PLP production emerged to overcome these limitations. Using genetic engineering, the *PLP1* gene is cloned into expression vectors (e.g., bacterial, insect, or mammalian systems) to produce purified PLP in vitro. Bacterial systems like *E. coli* offer cost-effective bulk production, while eukaryotic systems better replicate post-translational modifications, such as glycosylation, enhancing biological relevance.
PLP recombinant proteins are pivotal in studying demyelinating diseases. Mutations in *PLP1* are linked to Pelizaeus-Merzbacher disease (PMD), a fatal leukodystrophy, and are implicated in multiple sclerosis (MS) pathogenesis due to autoimmune responses against myelin proteins. Recombinant PLP enables in vitro modeling of these disorders, facilitating mechanistic studies, antibody-antigen interaction analyses, and drug screening. Additionally, it serves as an antigen in experimental autoimmune encephalomyelitis (EAE) models to mimic MS.
Beyond disease research, recombinant PLP aids in structural studies via X-ray crystallography or cryo-EM, revealing insights into myelin assembly and stability. Its applications extend to diagnostic tools for anti-myelin antibodies and potential therapeutic development. Despite technical hurdles in expression and purification, advancements in recombinant technology continue to expand PLP’s utility in neuroscience and translational medicine.
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