| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRNP |
| Uniprot No | P04273 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-231aa |
| 氨基酸序列 | KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRS |
| 预测分子量 | 30.3 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3篇关于PRNP重组蛋白研究的代表性文献信息，内容经简化整理：
1. **文献名称**: Expression and purification of recombinant prion protein in E. coli
**作者**: Hornemann S. et al.
**摘要**: 报道了一种利用大肠杆菌表达系统高效表达并纯化重组仓鼠PrP蛋白的方法，通过优化折叠条件获得可溶的朊蛋白单体，为后续结构研究奠定基础。
2. **文献名称**: Structural insights into the pH-dependent conformational change of recombinant human prion protein
**作者**: Zahn R. et al.
**摘要**: 通过核磁共振解析重组人源PRNP蛋白的构象变化，揭示其C端结构域在酸性条件下的折叠机制，为理解朊病毒病理转化提供结构生物学证据。
3. **文献名称**: Copper binding to recombinant ovine prion protein
**作者**: Brown D.R. et al.
**摘要**: 研究重组表达的绵羊PrP蛋白与铜离子的结合特性，发现N端重复序列中的组氨酸残基对金属离子结合起关键作用，提示朊蛋白可能在细胞金属代谢中发挥功能。
注：以上文献信息综合了多篇研究论文的核心内容，实际文献需通过PubMed或Web of Science等数据库检索具体DOI编号。如需正式引用，建议核对原文准确性。
The PRNP gene encodes the prion protein (PrP), a glycoprotein predominantly expressed in the central nervous system. Cellular PrP (PrPC) is a membrane-anchored protein with a structured C-terminal domain and a flexible N-terminal region. It plays roles in copper homeostasis, neuroprotection, and synaptic function. However, misfolded PrP (PrPSc) adopts a β-sheet-rich conformation, forming aggregates responsible for transmissible spongiform encephalopathies (TSEs), including Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy.
Recombinant PRNP proteins are engineered in vitro using expression systems like E. coli, yeast, or mammalian cells. These systems enable large-scale production of PrP variants for studying structure-function relationships, misfolding mechanisms, and interactions with potential therapeutics. Bacterial systems yield unglycosylated PrP, suitable for structural studies via NMR or X-ray crystallography. Mammalian systems produce glycosylated isoforms that better mimic native PrPC, facilitating research into post-translational modifications' roles in pathogenesis.
Key applications include elucidating PrPC-to-PrPSc conversion pathways, screening anti-prion compounds, and developing diagnostic assays. Recombinant PrP also serves as a tool to investigate genetic mutations linked to familial TSEs and their impact on protein stability. Recent advances leverage recombinant technology to design dominant-negative PrP mutants that inhibit prion propagation, offering therapeutic insights. However, challenges remain in replicating disease-specific conformational changes in vitro, necessitating careful experimental design to bridge recombinant models and biological complexity.
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