| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PFDN5 |
| Uniprot No | Q99471 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-154aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAQSINITELNLPQLEMLKNQLDQEVEFLS TSIAQLKVVQTKYVEAKD CLNVLNKSNEGKELLVPLTSSMYVPGKLHD VEHVLIDVGTGYYVEKTAEDAKDFFKRKIDFLTKQMEKIQPALQE KHA MKQAVMEMMSQKIQQLTALGAAQATAKA |
| 预测分子量 | 20 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PFDN5重组蛋白的3篇示例参考文献(注：文献为虚拟示例，实际研究中请核实真实来源)：
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1. **文献名称**: *"Recombinant PFDN5 promotes apoptosis in lung cancer cells via regulating Bcl-2/Bax pathway"*
**作者**: Zhang Y. et al. (2020)
**摘要**: 研究通过大肠杆菌表达系统纯化重组人PFDN5蛋白，发现其在肺癌细胞中过表达可激活线粒体凋亡通路，抑制肿瘤增殖，提示其潜在抗癌作用。
2. **文献名称**: *"Functional characterization of recombinant PFDN5 as a molecular chaperone in neurodegenerative models"*
**作者**: Liu X. et al. (2018)
**摘要**: 利用重组PFDN5蛋白在体外验证其与α-突触核蛋白的相互作用，证实其通过维持错误折叠蛋白的稳定性延缓帕金森病模型中的神经元退化。
3. **文献名称**: *"Development of a high-yield PFDN5 recombinant protein production system and its application in drug discovery"*
**作者**: Gupta R. et al. (2017)
**摘要**: 优化PFDN5在昆虫细胞中的重组表达工艺，获得高纯度蛋白，并用于筛选小分子抑制剂，以治疗与蛋白质错误折叠相关的遗传性疾病。
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**提示**：实际研究中建议通过PubMed或Web of Science检索关键词"PFDN5 recombinant protein"获取最新文献，重点关注其重组表达技术、结构解析或疾病机制研究。
**Background of PFDN5 Recombinant Protein**
PFDN5 (Prefoldin subunit 5), also known as MM-1 or C1orf55. is a member of the prefoldin chaperone family, which plays a critical role in cellular protein homeostasis. Prefoldin proteins act as molecular escorts, binding to nascent polypeptide chains to facilitate their proper folding or delivery to downstream chaperone systems like the cytosolic chaperonin CCT/TriC complex. PFDN5 specifically contributes to the stabilization and folding of cytoskeletal proteins, including actin and tubulin, ensuring their structural integrity and functionality.
Structurally, PFDN5 forms a hexameric complex with other prefoldin subunits, utilizing its coiled-coil and β-barrel domains to capture unfolded proteins. Recombinant PFDN5 is produced in vitro (e.g., in *E. coli* or mammalian expression systems) for functional studies. Its recombinant form retains the ability to bind misfolded proteins, suppress aggregation, and assist in refolding assays, making it valuable for investigating protein misfolding diseases like neurodegeneration or cancer.
Beyond its chaperone role, PFDN5 has been implicated in transcriptional regulation and tumor suppression. It interacts with oncoproteins such as c-Myc, modulating their stability and activity. Dysregulation of PFDN5 is linked to cancers, viral infections, and cellular stress responses, highlighting its therapeutic potential. Recombinant PFDN5 serves as a tool for elucidating these mechanisms, enabling drug discovery and biomarker development. Ongoing research aims to harness its chaperone activity for biotechnological and clinical applications.
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