| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PFDN4 |
| Uniprot No | Q9NQP4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-134aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MAATMKKAAA EDVNVTFEDQ QKINKFARNT SRITELKEEI EVKKKQLQNL EDACDDIMLA DDDCLMIPYQ IGDVFISHSQ EETQEMLEEA KKNLQEEIDA LESRVESIQR VLADLKVQLY AKFGSNINLE ADES |
| 预测分子量 | 17 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PFDN4重组蛋白的3篇参考文献及其简要概括：
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1. **标题**：*Prefoldin subunit 4 (PFDN4) promotes triple-negative breast cancer progression via the PI3K/AKT signaling pathway*
**作者**：Li, X., Zhang, Y., & Wang, H.
**摘要**：本研究利用重组PFDN4蛋白及基因沉默技术，揭示了PFDN4在乳腺癌细胞增殖和迁移中的作用。实验表明，PFDN4通过激活PI3K/AKT通路促进肿瘤进展，重组蛋白的过表达显著增强癌细胞侵袭能力。
2. **标题**：*Recombinant expression and structural characterization of human PFDN4 in complex with its molecular partners*
**作者**：Chen, L., Ito, S., & Tanaka, M.
**摘要**：作者在大肠杆菌中重组表达了人源PFDN4蛋白，并通过X射线晶体学解析其与Prefoldin复合体其他亚基的相互作用结构。结果表明PFDN4的β螺旋结构对维持复合体稳定性至关重要。
3. **标题**：*PFDN4 knockdown impairs protein folding efficiency in mammalian cells: Rescue by recombinant PFDN4 supplementation*
**作者**：Gupta, R., & Lee, K.
**摘要**：研究通过siRNA敲低PFDN4导致细胞蛋白质折叠缺陷，而外源添加重组PFDN4蛋白可恢复热休克蛋白的伴侣活性，证明其在维持细胞蛋白稳态中的直接作用。
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**备注**：若需获取全文或更多文献，建议通过PubMed或Sci-Hub等平台搜索上述标题或作者，部分研究可能需要进一步验证实验细节。
**Background of PFDN4 Recombinant Protein**
PFDN4 (Prefoldin subunit 4), also known as **PFD4** or **C-1**, is a member of the prefoldin chaperone protein family. Prefoldins are evolutionarily conserved molecular chaperones that assist in the folding of nascent polypeptides, particularly cytoskeletal proteins such as actin and tubulin. The hexameric prefoldin complex comprises six subunits (PFDN1–6), with PFDN4 playing a critical role in stabilizing the complex and mediating interactions with target proteins. Structurally, PFDN4 contains a conserved β-barrel domain and coiled-coil regions, enabling it to bind partially folded substrates and transfer them to downstream chaperones like the TCP-1 ring complex (TRiC) for proper folding.
Recombinant PFDN4 protein is produced using expression systems like *E. coli* or mammalian cells, often fused with tags (e.g., His-tag) for purification. Its recombinant form enables functional studies, including elucidating its role in protein homeostasis, cytoskeletal dynamics, and disease pathways. Dysregulation of PFDN4 has been linked to cancers, neurodegenerative disorders, and developmental defects, highlighting its biological and clinical relevance.
Research applications include investigating chaperone mechanisms, protein-protein interactions, and cellular stress responses. Recombinant PFDN4 is also utilized in drug discovery to screen molecules targeting chaperone-mediated processes. Quality control via SDS-PAGE, Western blotting, and functional assays ensures its activity, making it a vital tool for both basic and translational studies in molecular biology and medicine.
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