| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HNRPU |
| Uniprot No | Q00839 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-825aa |
| 氨基酸序列 | MSSSPVNVKKLKVSELKEELKKRRLSDKGLKAELMERLQAALDDEEAGGRPAMEPGNGSLDLGGDSAGRSGAGLEQEAAAGGDEEEEEEEEEEEGISALDGDQMELGEENGAAGAADSGPMEEEEAASEDENGDDQGFQEGEDELGDEEEGAGDENGHGEQQPQPPATQQQQPQQQRGAAKEAAGKSSGPTSLFAVTVAPPGARQGQQQAGGKKKAEGGGGGGRPGAPAAGDGKTEQKGGDKKRGVKRPREDHGRGYFEYIEENKYSRAKSPQPPVEEEDEHFDDTVVCLDTYNCDLHFKISRDRLSASSLTMESFAFLWAGGRASYGVSKGKVCFEMKVTEKIPVRHLYTKDIDIHEVRIGWSLTTSGMLLGEEEFSYGYSLKGIKTCNCETEDYGEKFDENDVITCFANFESDEVELSYAKNGQDLGVAFKISKEVLAGRPLFPHVLCHNCAVEFNFGQKEKPYFPIPEEYTFIQNVPLEDRVRGPKGPEEKKDCEVVMMIGLPGAGKTTWVTKHAAENPGKYNILGTNTIMDKMMVAGFKKQMADTGKLNTLLQRAPQCLGKFIEIAARKKRNFILDQTNVSAAAQRRKMCLFAGFQRKAVVVCPKDEDYKQRTQKKAEVEGKDLPEHAVLKMKGNFTLPEVAECFDEITYVELQKEEAQKLLEQYKEESKKALPPEKKQNTGSKKSNKNKSGKNQFNRGGGHRGRGGFNMRGGNFRGGAPGNRGGYNRRGNMPQRGGGGGGSGGIGYPYPRAPVFPGRGSYSNRGNYNRGGMPNRGNYNQNFRGRGNNRGYKNQSQGYNQWQQGQFWGQKPWSQHYHQGYY |
| 预测分子量 | 90,5 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HNRPU重组蛋白的3篇参考文献示例(注：以下文献为虚构示例，仅供参考格式和内容方向)：
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1. **文献名称**: *HNRPU/SAF-A facilitates DNA repair through chromatin remodeling*
**作者**: Smith, J., et al. (2015)
**摘要**: 本研究利用重组HNRPU蛋白，揭示了其在DNA损伤应答中的作用机制。通过体外实验证明，HNRPU通过结合损伤位点并招募染色质重塑复合物(如SWI/SNF)，促进同源重组修复。研究为HNRPU在基因组稳定性中的功能提供了新见解。
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2. **文献名称**: *Efficient prokaryotic expression and purification of recombinant HNRPU for functional studies*
**作者**: Johnson, R., et al. (2018)
**摘要**: 作者开发了一种在大肠杆菌中高效表达重组HNRPU蛋白的方法，并优化了纯化步骤以获得高纯度蛋白。通过凝胶迁移实验(EMSA)验证了重组蛋白的RNA结合活性，为后续研究HNRPU的分子互作提供了可靠工具。
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3. **文献名称**: *HNRPU interacts with HIV-1 RNA to modulate viral replication*
**作者**: Lee, S., et al. (2020)
**摘要**: 该研究利用重组HNRPU蛋白，发现其直接结合HIV-1 RNA的特定区域，并调控病毒转录后加工。敲低HNRPU显著抑制病毒复制，表明其作为潜在抗病毒治疗靶点的可能性。
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4. **文献名称**: *Oncogenic role of HNRPU in breast cancer via regulating alternative splicing*
**作者**: Chen, X., et al. (2022)
**摘要**: 通过重组HNRPU蛋白及CRISPR技术，研究者发现HNRPU通过调控致癌基因(如MYC)的可变剪接，促进乳腺癌细胞增殖和转移。靶向HNRPU可逆转肿瘤表型，提示其作为治疗靶点的潜力。
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**备注**：以上文献为示例性质，实际研究中请通过PubMed、Web of Science等数据库检索真实文献。
**Background of HNRNPU Recombinant Protein**
HNRNPU (heterogeneous nuclear ribonucleoprotein U), also known as UP1 or SAF-A (scaffold attachment factor A), is a multifunctional RNA/DNA-binding protein involved in chromatin organization, transcriptional regulation, and mRNA processing. As a member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family, HNRNPU plays critical roles in cellular processes such as RNA splicing, stability, and transport, as well as maintaining nuclear architecture by interacting with scaffold/matrix attachment regions (S/MARs) of DNA.
The recombinant HNRNPU protein is engineered through molecular cloning techniques, typically expressed in *E. coli* or mammalian cell systems*,* followed by purification to homogeneity. Structurally, it contains an N-terminal SAP (SAF-A/B, Acinus, PIAS) domain for DNA binding, two RNA recognition motifs (RRMs), and a C-terminal disordered region rich in arginine and glycine residues, which mediates protein-protein interactions. Dysregulation of HNRNPU is linked to neurodevelopmental disorders, cancers, and viral infections, highlighting its biomedical relevance.
Recombinant HNRNPU serves as a vital tool for *in vitro* studies, enabling researchers to dissect its molecular interactions, RNA/DNA-binding specificity, and role in liquid-liquid phase separation (LLPS) associated with nuclear condensate formation. It is also used to investigate HNRNPU’s involvement in diseases, such as its oncogenic potential in glioblastoma or its role in Zika virus replication. Challenges in studying HNRNPU include understanding context-dependent post-translational modifications (e.g., phosphorylation) and its dynamic interplay with non-coding RNAs. Continued research on recombinant HNRNPU aims to uncover therapeutic targets for related pathologies.
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