| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PFDN2 |
| Uniprot No | Q9UHV9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-154aa |
| 氨基酸序列 | MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS |
| 预测分子量 | 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PFDN2重组蛋白的3篇参考文献及其摘要概述：
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1. **文献名称**: *Prefoldin 2 regulates mitochondrial function and modulates glioma cell growth*
**作者**: Zhang Y, et al. (2018)
**摘要**: 该研究通过重组PFDN2蛋白体外实验，发现其在胶质瘤细胞中通过调控线粒体能量代谢通路(如OXPHOS)抑制肿瘤增殖。PFDN2的过表达可诱导细胞周期阻滞，提示其作为潜在肿瘤治疗靶点。
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2. **文献名称**: *Recombinant PFDN2 inhibits α-synuclein aggregation in Parkinson’s disease models*
**作者**: Chen L, et al. (2020)
**摘要**: 研究利用大肠杆菌表达系统制备重组人源PFDN2蛋白，并证明其通过分子伴侣功能抑制α-突触核蛋白异常聚集。在帕金森病细胞模型中，外源性添加PFDN2显著减少神经元凋亡。
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3. **文献名称**: *Structural and functional characterization of PFDN2 in ribosome biogenesis*
**作者**: Wang X, et al. (2016)
**摘要**: 通过重组表达和纯化PFDN2蛋白，结合冷冻电镜分析，揭示了其与前折叠蛋白复合体协作参与核糖体RNA加工的结构基础。研究为PFDN2在蛋白质合成质量控制中的作用提供机制解释。
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**提示**：以上文献信息为基于领域知识的模拟，实际引用时请通过PubMed或Web of Science检索最新实证研究。若需具体论文，建议使用关键词“PFDN2 recombinant protein”或“PFDN2 AND gene cloning”进行精准查询。
**Background of PFDN2 Recombinant Protein**
PFDN2 (Prefoldin subunit 2), a member of the prefoldin chaperone family, plays a critical role in cellular protein homeostasis by assisting in the folding and stabilization of newly synthesized polypeptides, particularly cytoskeletal components like actin and tubulin. Prefoldin complexes, composed of six subunits (PFDN1-6), act as molecular chaperones by capturing unfolded proteins and transferring them to group II chaperonins (e.g., CCT complex) for proper folding. PFDN2 is highly conserved across eukaryotes and is ubiquitously expressed, underscoring its essential function in maintaining cellular integrity.
Structurally, PFDN2 contains a coiled-coil domain that facilitates interactions with other prefoldin subunits and client proteins. Dysregulation of PFDN2 has been implicated in various diseases, including cancers and neurodegenerative disorders. For instance, altered PFDN2 expression correlates with tumor progression, potentially influencing cell proliferation, migration, or apoptosis. In neurodegenerative contexts, impaired protein folding linked to PFDN2 dysfunction may contribute to the aggregation of misfolded proteins, a hallmark of diseases like Alzheimer’s.
Recombinant PFDN2 protein, typically produced in *E. coli* or mammalian expression systems, enables detailed biochemical and functional studies. Its applications span structural analysis (e.g., X-ray crystallography), *in vitro* chaperone activity assays, and exploration of its interactions with partner proteins or nucleic acids. Additionally, recombinant PFDN2 serves as an antigen for antibody development or a tool to investigate its role in cellular pathways, such as stress response or cytoskeletal dynamics.
Overall, PFDN2 recombinant protein is a vital resource for deciphering the molecular mechanisms of protein folding, disease pathogenesis, and therapeutic target validation.
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