纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | HNRNPA1 |
Uniprot No | P09651-2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-320aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSKSESP KEPEQLRKLF IGGLSFETTD ESLRSHFEQW GTLTDCVVMR DPNTKRSRGF GFVTYATVEE VDAAMNARPH KVDGRVVEPK RAVSREDSQR PGAHLTVKKI FVGGIKEDTE EHHLRDYFEQ YGKIEVIEIM TDRGSGKKRG FAFVTFDDHD SVDKIVIQKY HTVNGHNCEV RKALSKQEMA SASSSQRGRS GSGNFGGGRG GGFGGNDNFG RGGNFSGRGG FGGSRGGGGY GGSGDGYNGF GNDGSNFGGG GSYNDFGNYN NQSSNFGPMK GGNFGGRSSG PYGGGGQYFA KPRNQGGYGG SSSSSSYGSG RRF |
预测分子量 | 37 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HNRNPA1重组蛋白的3篇参考文献(名称、作者及摘要概括):
1. **"HnRNP A1 regulates alternative splicing of tau exon 10 by targeting RNA stem-loop structures"**
- **作者**: D’Souza I, et al.
- **摘要**: 该研究利用重组HNRNPA1蛋白,揭示了其通过结合tau前体mRNA的特定茎环结构调控tau外显子10的选择性剪接,可能与神经退行性疾病中tau蛋白异常异构体形成相关。
2. **"Phase separation by low complexity domains of hnRNPA1 drives aggregation in ALS/FTD"**
- **作者**: Lin Y, et al.
- **摘要**: 通过体外重组蛋白实验,发现HNRNPA1的低复杂度结构域(LCD)在液-液相分离中起关键作用,其突变体(如D262V)异常聚集可能导致肌萎缩侧索硬化症(ALS)等疾病的病理机制。
3. **"Structural basis of HNRNPA1 recognition of pre-miRNA for Dicer processing"**
- **作者**: Xu C, et al.
- **摘要**: 该研究解析了重组HNRNPA1蛋白结合pre-miRNA的晶体结构,阐明其通过RRM结构域特异性识别RNA,并辅助Dicer酶对miRNA前体的切割成熟过程。
如需扩展,可补充疾病相关或药物筛选研究文献。
**Background of HNRNPA1 Recombinant Protein**
Heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) is a ubiquitously expressed RNA-binding protein belonging to the hnRNP family, which plays critical roles in RNA metabolism. It is involved in mRNA splicing, transport, stability, and translation by interacting with specific RNA sequences or structures. HNRNPA1 contains two N-terminal RNA recognition motifs (RRMs) responsible for RNA binding and a C-terminal prion-like domain (PrLD) implicated in protein-protein interactions and liquid-liquid phase separation. Dysregulation of HNRNPA1 is linked to neurodegenerative diseases (e.g., ALS, FTLD) and cancers, where mutations in its PrLD promote pathological aggregation or alter RNA processing.
Recombinant HNRNPA1 protein is engineered for *in vitro* studies to dissect its molecular functions. It is typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems, purified via affinity tags (e.g., His-tag), and validated for RNA-binding activity. Researchers use it to study RNA-protein interactions, splicing mechanisms, and phase separation dynamics. In disease contexts, recombinant HNRNPA1 helps model aggregation behavior caused by ALS/FTLD-linked mutations (e.g., D262V) and test therapeutic strategies targeting aberrant phase transitions. Additionally, it serves as a tool for structural studies (e.g., crystallography, NMR) and high-throughput drug screening to identify modulators of HNRNPA1 function. Its role in cancer—regulating oncogene (e.g., MYC) splicing or acting as a tumor suppressor—is also explored using recombinant variants. Overall, HNRNPA1 recombinant protein is vital for advancing mechanistic and translational research in RNA biology and protein aggregation disorders.
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