| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | hupA |
| Uniprot No | P0ACF1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-90aa |
| 氨基酸序列 | MNKTQLIDVIAEKAELSKTQAKAALESTLAAITESLKEGDAVQLVGFGTFKVNHRAERTGRNPQTGKEIKIAAANVPAFVSGKALKDAVK |
| 预测分子量 | 11.0 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hupA重组蛋白的3-4篇参考文献示例(内容为虚构，仅作格式参考)：
1. **文献名称**: "Expression and Purification of Recombinant hupA Protein from Halophilic Archaea"
**作者**: Zhang L. et al.
**摘要**: 研究报道了从极端嗜盐古菌中克隆hupA基因，并利用大肠杆菌表达系统成功表达重组HupA蛋白。通过优化诱导条件和纯化步骤(如离子交换层析)，获得高纯度蛋白，证实其具有DNA结合活性，可能参与染色质结构调控。
2. **文献名称**: "Structural Characterization of hupA Recombinant Protein and Its Role in DNA Compaction"
**作者**: Tanaka K., Smith R.
**摘要**: 通过X射线晶体学解析了重组HupA蛋白的三维结构，发现其具有典型的组蛋白折叠结构域。体外实验表明，HupA可通过非特异性结合DNA促进超螺旋形成，提示其在维持基因组稳定性中的功能。
3. **文献名称**: "Functional Analysis of hupA in Bacterial Stress Response Using Recombinant Protein"
**作者**: Gupta S. et al.
**摘要**: 构建了重组HupA蛋白突变体，研究其在氧化应激和高温环境下的DNA保护作用。结果显示，HupA通过增强DNA的抗损伤能力，显著提高宿主菌的环境适应性。
4. **文献名称**: "Development of a hupA-Based Affinity Tag for Nucleic Acid Purification"
**作者**: Chen W. et al.
**摘要**: 提出将重组HupA蛋白作为新型亲和标签，用于快速纯化质粒DNA。实验证明，HupA标签系统具有高特异性且兼容常规表达宿主，为分子生物学工具开发提供了新思路。
(注：以上文献为模拟内容，实际研究中请通过学术数据库检索具体文献。)
**Background of HupA Recombinant Protein**
The HupA (Histone-like UV-stress protein A) recombinant protein is derived from bacterial histone-like proteins, particularly studied in pathogens like *Mycobacterium tuberculosis* (Mtb). These proteins are structurally and functionally analogous to eukaryotic histones, playing critical roles in DNA compaction, replication, and stress response. HupA, specifically, is a small, basic protein that binds DNA with high affinity, stabilizing chromosomal architecture under environmental stressors such as oxidative damage, UV radiation, or nutrient deprivation.
In Mtb, HupA is implicated in bacterial survival during host infection, aiding adaptation to the hostile intracellular environment of macrophages. Its ability to regulate DNA topology and gene expression makes it essential for pathogenicity and persistence. Recombinant HupA is engineered via heterologous expression systems (e.g., *E. coli*), enabling large-scale production for functional studies. Researchers utilize purified HupA to investigate its DNA-binding mechanisms, structural dynamics (e.g., dimerization, DNA interaction domains), and role in stress adaptation.
Interest in HupA also stems from its potential as a diagnostic or therapeutic target. Epitopes of HupA may serve as antigens for tuberculosis (TB) diagnostics or vaccine development, given its immunogenicity in host immune responses. Additionally, structural insights into HupA-DNA complexes could inform novel antimicrobial strategies targeting bacterial chromatin organization.
Overall, HupA recombinant protein serves as a vital tool for unraveling microbial pathogenesis, stress response pathways, and developing interventions against infections like TB. Its study bridges molecular microbiology and translational medicine, highlighting the importance of chromatin-associated proteins in bacterial survival and virulence.
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