| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | hup |
| Uniprot No | P0C0H2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-91aa |
| 氨基酸序列 | MANKQDLIAKVAEATELTKKDSAAAVDAVFSTIEAFLAEGEKVQLIGFGNFEVRERAARKGRNPQTGAEIEIAASKVPAFKAGKALKDAVK |
| 预测分子量 | 17.1 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“Hup重组蛋白”的虚构参考文献示例(仅供参考，非真实文献)：
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1. **标题**：*Expression and Purification of Recombinant Hup Protein in E. coli*
**作者**：Smith A, et al.
**期刊**：Protein Expression and Purification, 2020.
**摘要**：研究通过大肠杆菌系统高效表达Hup重组蛋白，优化诱导条件并采用镍柱亲和层析纯化，验证其与DNA结合活性，为后续功能研究提供基础。
2. **标题**：*Structural Insights into Hup Recombinant Protein by Cryo-EM*
**作者**：Zhang L, et al.
**期刊**：Journal of Structural Biology, 2021.
**摘要**：利用冷冻电镜解析Hup重组蛋白的三维结构，揭示其保守结构域及潜在的DNA结合位点，为阐明其在基因调控中的作用机制提供依据。
3. **标题**：*Hup Recombinant Protein as a Novel Vaccine Adjuvant in Murine Models*
**作者**：Johnson R, et al.
**期刊**：Biotechnology Reports, 2019.
**摘要**：评估Hup重组蛋白作为疫苗佐剂的免疫增强效果，实验显示其可显著提高抗原特异性抗体水平，提示其在疫苗开发中的应用潜力。
4. **标题**：*Functional Analysis of Hup Protein in Bacterial DNA Repair Pathways*
**作者**：Lee S, et al.
**期刊**：Cellular & Molecular Biology Letters, 2022.
**摘要**：通过基因敲除和重组蛋白回补实验，证明Hup蛋白参与细菌DNA损伤修复过程，可能通过调控重组酶活性维持基因组稳定性。
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如需真实文献，建议通过PubMed、Google Scholar等平台检索关键词“Hup recombinant protein”或“Hup protein recombination”。部分研究可能涉及“Hup”在特定物种(如固氮菌*Bradyrhizobium*)中的重组表达及功能分析。
**Background of HU Recombinant Protein**
HU proteins, originally identified in *Escherichia coli*, are small, abundant DNA-binding proteins belonging to the histone-like protein family. They play a critical role in bacterial nucleoid organization, DNA replication, repair, and recombination. Structurally, HU proteins form homodimers or heterodimers (e.g., HUαβ in *E. coli*) that bind nonspecifically to DNA, inducing bends or stabilizing distorted DNA conformations. Their ability to compact DNA and modulate chromatin-like structures has drawn parallels to eukaryotic histones, though they lack sequence specificity.
The term "HU recombinant protein" refers to engineered versions of these proteins produced via heterologous expression systems, such as *E. coli* or yeast. Recombinant production allows scalable, high-purity yields for functional studies and applications. Researchers leverage recombinant HU proteins to dissect their roles in DNA dynamics, nucleoid architecture, and stress responses in bacteria. Beyond basic science, HU proteins have biotechnological relevance. Their DNA-stabilizing properties are exploited in *in vitro* DNA manipulation, such as enhancing PCR efficiency or stabilizing plasmids during cloning.
Interest in HU proteins extends to medical research. Some pathogens, like *Mycobacterium tuberculosis*, rely on HU homologs (e.g., HupB) for virulence and persistence, making them potential drug targets. Additionally, recombinant HU proteins are explored as adjuvants in vaccines or tools for synthetic biology due to their DNA-condensing abilities. Challenges remain in optimizing expression systems to ensure proper folding and post-translational modifications, particularly for eukaryotic applications. Overall, HU recombinant proteins serve as versatile tools bridging structural biology, microbiology, and biotechnology, with ongoing research expanding their utility in both fundamental and applied contexts.
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