| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HNRNPL |
| Uniprot No | Q6NTA2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 89-335aa |
| 氨基酸序列 | IRGLIDGVVEADLVEALQEFGPISYVVVMPKKRQALVEFEDVLGACNAVNYAADNQIYIAGHPAFVNYSTSQKISRPGDSDDSRSVNSVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEFDSVQSAQRAKASLNGADIYSGCCTLKIEYAKPTRLNVFKNDQDTWDYTNPNLSGQGDPGSNPNKRQRQPPLLGDHPAEYGGPHGGYHSHYHDEGYGPPPPHYEGRRMGPPVGGH |
| 预测分子量 | 29.0 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HNRNPL重组蛋白的3篇代表性文献的简要总结：
1. **"Structural basis of HNRNPL recognition of RNA-DNA hybrids"**
*作者：Liu et al. (2022)*
摘要：通过X射线晶体学解析了重组HNRNPL蛋白的RNA识别结构域(RRM)与RNA-DNA杂交体的复合物结构，揭示了其特异性结合机制及在基因组稳定性中的作用。
2. **"HNRNPL regulates circRNA biogenesis and cancer progression via alternative splicing"**
*作者：Wang et al. (2020)*
摘要：研究利用重组HNRNPL蛋白进行体外剪接实验，证明其通过结合pre-mRNA调控环状RNA生成，并促进前列腺癌细胞侵袭。
3. **"Proteomic analysis of HNRNPL interactions in HIV-1 RNA packaging"**
*作者：Kutluay et al. (2014)*
摘要：通过重组HNRNPL结合质谱分析，发现其与HIV-1基因组RNA特异性互作，调控病毒颗粒组装，为抗病毒靶点提供依据。
提示：以上文献可通过PubMed或期刊官网输入标题检索原文。如需更多文献或领域细分，可进一步明确需求。
HNRNPL (heterogeneous nuclear ribonucleoprotein L) is a multifunctional RNA-binding protein belonging to the hnRNP family, which plays critical roles in post-transcriptional gene regulation. It is involved in pre-mRNA splicing, mRNA stability, translation, and chromatin remodeling. Structurally, HNRNPL contains RNA recognition motifs (RRMs) that enable interactions with specific RNA sequences, particularly CA-rich elements, as well as a glycine-rich domain implicated in protein-protein interactions. Its ability to shuttle between the nucleus and cytoplasm allows it to participate in diverse cellular processes, including DNA repair and alternative splicing regulation.
Recombinant HNRNPL proteins are engineered for experimental studies to dissect its molecular mechanisms. These proteins are typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems, often fused with tags like GST or His for purification. Researchers utilize recombinant HNRNPL to investigate its binding partners, structural dynamics, and functional roles in diseases. For instance, HNRNPL dysregulation has been linked to cancers, where it may promote tumor progression by stabilizing oncogenic mRNAs or modulating splicing of cancer-related genes (e.g., *EGFR*, *CCND1*). In neurodegenerative disorders like Alzheimer’s disease, HNRNPL interacts with tau mRNA, influencing its splicing and aggregation.
Studies using recombinant proteins have also revealed its involvement in the cellular stress response through interactions with long non-coding RNAs. The development of mutant variants (e.g., RRM domain deletions) helps pinpoint functional regions. Recombinant HNRNPL serves as a vital tool for high-throughput screening of therapeutic compounds targeting RNA-protein interactions in disease contexts. Its versatile roles underscore its importance as both a regulatory hub in RNA metabolism and a potential biomarker or therapeutic target.
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