| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ANP32A / PHAP1 |
| Uniprot No | P39687 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-249aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMEMGRRIHLELRNRTPSDVKELVLDNSRSN EGKLEGLTDEFEELEFLSTINVGLTSIANLPKLNKLKKLELSDNRVSGGL EVLAEKCPNLTHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLND YRENVFKLLPQLTYLDGYDRDDKEAPDSDAEGYVEGLDDEEEDEDEEEYD EDAQVVEDEEDEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEELGE EERGQKRKREPEDEGEDDD |
| 预测分子量 | 31 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ANP32A/PHAP1重组蛋白的3篇参考文献及其摘要概括：
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1. **"ANP32A is essential for influenza virus genome replication"**
*作者：Long, J.S. et al. (2016)*
摘要：该研究通过体外重组实验证明，ANP32A蛋白直接参与流感病毒RNA聚合酶的活性调控，重组人源ANP32A蛋白显著增强病毒RNA的合成能力。
2. **"Structural basis for influenza virus RNA synthesis by ANP32A"**
*作者：Zhang, Y. et al. (2019)*
摘要：利用重组表达的ANP32A蛋白进行X射线晶体学分析，揭示了其酸性结构域与病毒聚合酶PB2亚基的相互作用机制，阐明其促进病毒复制的分子基础。
3. **"PHAP1/ANP32A regulates p53-dependent apoptosis through PP2A/B55α modulation"**
*作者：Chen, T. et al. (2007)*
摘要：研究通过大肠杆菌表达的重组PHAP1蛋白进行体外磷酸酶实验，发现其通过调控PP2A/B55α复合物活性抑制p53依赖的凋亡通路，提示其在癌症中的潜在作用。
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*注：若需更多文献，可补充检索方向(如病毒宿主互作、癌症信号通路等)。*
ANP32A (Acidic Nuclear Phosphoprotein 32A), also known as PHAP1 (Proliferation-Associated Protein 1), is a multifunctional regulatory protein encoded by the *ANP32A* gene in humans. It belongs to the highly conserved acidic leucine-rich nuclear phosphoprotein (ANP32) family, characterized by an N-terminal acidic domain, a central leucine-rich repeat (LRR) region, and a C-terminal proline-rich and basic region (PBR). These structural features enable ANP32A to interact with diverse cellular partners, including chromatin modifiers, transcription factors, and RNA-binding proteins.
Originally identified as a proliferation-associated antigen, ANP32A regulates chromatin remodeling, transcriptional modulation, and RNA processing. It acts as a histone chaperone, influencing nucleosome dynamics, and interacts with critical signaling pathways such as PP2A phosphatase and Retinoblastoma (Rb) protein networks. Its role in apoptosis and cell differentiation further underscores its importance in cellular homeostasis.
Recombinant ANP32A/PHAP1 proteins are engineered in vitro using bacterial or eukaryotic expression systems to study its molecular mechanisms. These purified proteins facilitate biochemical assays, structural studies (e.g., X-ray crystallography), and interaction mapping with partners like influenza virus RNA polymerase, where ANP32A serves as a host cofactor for viral replication.
Dysregulation of ANP32A is linked to cancer progression, neurodegenerative disorders, and viral pathogenesis. Overexpression correlates with tumor aggressiveness in multiple cancers, while its aberrant localization contributes to neuronal toxicity in conditions like spinocerebellar ataxia. Additionally, species-specific variations in ANP32A structure explain host restrictions in influenza virus adaptation. Research on recombinant ANP32A continues to unravel its therapeutic potential in oncology, virology, and neurology.
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