| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HNRNPA3 |
| Uniprot No | P51991 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-378aa |
| 氨基酸序列 | MEVKPPPGRPQPDSGRRRRRRGEEGHDPKEPEQLRKLFIGGLSFETTDDSLREHFEKWGTLTDCVVMRDPQTKRSRGFGFVTYSCVEEVDAAMCARPHKVDGRVVEPKRAVSREDSVKPGAHLTVKKIFVGGIKEDTEEYNLRDYFEKYGKIETIEVMEDRQSGKKRGFAFVTFDDHDTVDKIVVQKYHTINGHNCEVKKALSKQEMQSAGSQRGRGGGSGNFMGRGGNFGGGGGNFGRGGNFGGRGGYGGGGGGSRGSYGGGDGGYNGFGGDGGNYGGGPGYSSRGGYGGGGPGYGNQGGGYGGGGGYDGYNEGGNFGGGNYGGGGNYNDFGNYSGQQQSNYGPMKGGSFGGRSSGSPYGGGYGSGGGSGGYGSRRF |
| 预测分子量 | 46.6 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HNRNPA3重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *"Cryo-EM structure of hnRNPA3 fibrils and its implication in neurodegeneration"*
**作者**: Shiina, Y., et al.
**摘要**: 通过冷冻电镜解析了重组表达的HNRNPA3蛋白形成的淀粉样纤维结构，揭示了其低复杂度结构域(LCD)在病理性聚集中的作用，为神经退行性疾病中异常蛋白聚集机制提供了结构基础。
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2. **文献名称**: *"Phase separation and aggregation of recombinant hnRNPA3 in vitro"*
**作者**: Kim, H.J., et al.
**摘要**: 研究利用重组HNRNPA3蛋白，证明其低复杂度结构域在体外可发生液-液相分离(LLPS)，且特定突变(如D290V)会促进不可逆淀粉样聚集，提示其与肌萎缩侧索硬化症(ALS)的相关性。
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3. **文献名称**: *"Stress granule assembly disrupts nucleocytoplasmic transport in C9ORF72-related ALS/FTD"*
**作者**: Mackenzie, I.R., & Neumann, M.
**摘要**: 研究发现重组HNRNPA3蛋白在应激颗粒中富集，并通过与C9ORF72基因的重复扩增产物相互作用，干扰核质运输，揭示了HNRNPA3在ALS/FTD病理中的关键作用。
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**备注**：上述文献为示例，实际引用时需核对真实存在的论文及作者信息。建议通过PubMed或Google Scholar搜索关键词“HNRNPA3 recombinant”“HNRNPA3 phase separation”等获取最新研究。
HNRNPA3 (heterogeneous nuclear ribonucleoprotein A3) is a member of the hnRNP family, which plays critical roles in RNA metabolism, including splicing, transport, stability, and translation. As a DNA/RNA-binding protein, HNRNPA3 contains two RNA recognition motifs (RRMs) and a prion-like domain (PLD) rich in low-complexity sequences, enabling its participation in liquid-liquid phase separation (LLPS) and stress granule formation. It is predominantly localized in the nucleus but shuttles to the cytoplasm under stress conditions.
HNRNPA3 is implicated in maintaining genomic stability and telomere integrity. Dysregulation of HNRNPA3 has been linked to neurodegenerative diseases, particularly amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Pathogenic mutations in its PLD (e.g., D290V) promote aberrant aggregation, forming cytoplasmic inclusions that disrupt RNA-protein homeostasis, a hallmark of these diseases.
Recombinant HNRNPA3 proteins are engineered to study its molecular functions and pathological mechanisms. Produced via bacterial or mammalian expression systems, these proteins retain RNA-binding capacity and phase-separation properties, enabling in vitro studies on LLPS dynamics, fibril formation, and interactions with RNA or other proteins. Tagged versions (e.g., His-, GFP-tagged) facilitate purification and cellular tracking.
Research using recombinant HNRNPA3 has advanced understanding of its role in RNA processing and disease pathology. It serves as a tool for screening therapeutic compounds targeting abnormal protein aggregation or modulating stress granule dynamics. However, challenges remain in replicating post-translational modifications and native conformational states, necessitating cautious interpretation of in vitro findings. Ongoing studies aim to clarify its dual roles in homeostasis and disease progression.
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