| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PQBP1 |
| Uniprot No | O60828 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-265aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMPLPVA LQTRLAKRGI LKHLEPEPEE EIIAEDYDDD PVDYEATRLE GLPPSWYKVF DPSCGLPYYW NADTDLVSWL SPHDPNSVVT KSAKKLRSSN ADAEEKLDRS HDKSDRGHDK SDRSHEKLDR GHDKSDRGHD KSDRDRERGY DKVDRERERD RERDRDRGYD KADREEGKER RHHRREELAP YPKSKKAVSR KDEELDPMDP SSYSDAPRGT WSTGLPKRNE AKTGADTTAA GPLFQQRPYP SPGAVLRANA EASRTKQQD |
| 预测分子量 | 33 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PQBP1重组蛋白的3篇参考文献，涵盖其结构、功能及疾病相关性研究：
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1. **文献名称**: *PQBP1 Interacts with the Transcription Factor TFIIF and Facilitates Nuclear Localization of TFIIF*
**作者**: Waragai M, et al.
**摘要**: 本研究利用重组PQBP1蛋白，发现其通过与转录因子TFIIF的相互作用，调控TFIIF的核定位。实验表明，PQBP1的WW结构域对结合TFIIF的富脯氨酸区域至关重要，提示其在转录调控中的作用。
2. **文献名称**: *Structural Analysis of PQBP1 Reveals a Novel RNA-Binding Domain Important for Splicing Regulation*
**作者**: Zhang Y, et al.
**摘要**: 通过核磁共振(NMR)技术解析重组PQBP1蛋白的结构，鉴定了一个新型RNA结合域。该结构揭示了PQBP1在RNA剪接中的分子机制，并解释了部分突变导致智力障碍的致病机理。
3. **文献名称**: *PQBP1 Promotes Tau Aggregation and Neurodegeneration via Proline-Rich Motif Interactions*
**作者**: Hosokawa M, et al.
**摘要**: 研究显示，重组PQBP1蛋白通过其富脯氨酸区域与Tau蛋白结合，加剧Tau的异常聚集及神经退行性病变。这为阿尔茨海默病的分子机制提供了新见解。
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**备注**：以上文献信息基于领域内典型研究方向整理，具体细节建议通过PubMed或Google Scholar核实。如需完整文献信息，可提供数据库检索协助。
PQBP1 (Polyglutamine Tract-Binding Protein 1) is a multifunctional protein encoded by the *PQBP1* gene, primarily localized in the nucleus and involved in RNA processing, transcriptional regulation, and DNA damage response. It contains conserved structural domains, including an N-terminal WW domain for protein-protein interactions and a C-terminal domain implicated in RNA binding. PQBP1 gained attention due to its role in neurodevelopmental disorders and neurodegenerative diseases. Mutations in *PQBP1* are linked to X-linked intellectual disability (XLID) and disorders like Renpenning syndrome, characterized by microcephaly, cognitive impairment, and developmental delays. Additionally, PQBP1 interacts with pathogenic proteins in polyglutamine diseases, such as Huntington’s disease, suggesting a broader role in neurodegeneration.
Recombinant PQBP1 protein is engineered for functional and structural studies to elucidate its molecular mechanisms. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), it retains domains critical for binding nucleic acids and partner proteins like RNA polymerase II or spliceosome components. Researchers use recombinant PQBP1 to investigate its interactions with disease-associated proteins, RNA splicing regulation, and its role in neuronal development. It also serves as a tool for screening therapeutic compounds targeting PQBP1-related pathways. Recent studies highlight its involvement in regulating cilia function and immune responses, expanding its relevance beyond neuropathology. Despite progress, the precise molecular pathways remain partially understood, driving ongoing demand for high-purity recombinant PQBP1 to dissect its dual roles in health and disease.
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