| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | hupB |
| Uniprot No | Q9KHS6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-90aa |
| 氨基酸序列 | MNKSELIDAIAASADLPKAAAGRALDAVIESVTGALKAGDSVVLVGFGTFSVTDRPARIGRNPQTGKTLEIAAAKKPGFKAGKALKEAVN |
| 预测分子量 | 22.1 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3篇关于HupB重组蛋白的假设参考文献(基于领域内常见研究方向模拟，建议核实真实文献)：
1. **"Recombinant HupB from Mycobacterium tuberculosis: Cloning, Expression, and Purification"**
- 作者：A. Kumar et al.
- 摘要：报道了结核分枝杆菌hupB基因的克隆及在大肠杆菌中的重组表达，优化了纯化条件，并通过质谱验证蛋白完整性，为后续功能研究奠定基础。
2. **"DNA-binding Properties of HupB: A Key Nucleoid-Associated Protein in Mycobacterial Latency"**
- 作者：S. Chakraborty & L. Cole
- 摘要：通过体外实验证明重组HupB蛋白以序列非依赖性方式结合DNA，并参与分枝杆菌休眠期染色质压缩，提示其在细菌潜伏感染中的调控作用。
3. **"Immunogenicity of Recombinant HupB in Tuberculosis Vaccine Development"**
- 作者：M. Singh et al.
- 摘要：评估重组HupB蛋白在小鼠模型中的免疫原性，显示其可诱导Th1型免疫反应，提示其作为结核病亚单位疫苗候选分子的潜力。
(注：以上为模拟内容，实际文献需通过PubMed/Google Scholar检索关键词如"HupB recombinant protein Mycobacterium"等获取。)
**Background of HupB Recombinant Protein**
HupB, a histone-like protein, is primarily associated with bacterial species, notably *Mycobacterium tuberculosis* (Mtb), the causative agent of tuberculosis. Functionally analogous to eukaryotic histones, HupB plays a critical role in organizing and compacting bacterial DNA, thereby regulating gene expression and maintaining chromosomal integrity. In mycobacteria, it is encoded by the *hupB* gene (Rv2986c) and is implicated in stress adaptation, dormancy, and pathogenicity. Studies suggest HupB contributes to Mtb’s ability to persist in hostile host environments, such as hypoxia or nutrient deprivation, by modulating DNA topology and facilitating transcriptional adjustments during latency.
Structurally, HupB contains two conserved domains: an N-terminal domain responsible for DNA binding and oligomerization, and a flexible C-terminal domain enriched in alanine and proline residues, which may mediate protein-protein interactions or phase separation. Its role in mycobacterial physiology extends to potential involvement in redox homeostasis and cell wall processes, making it a target for investigating virulence mechanisms.
Recombinant HupB protein is produced via heterologous expression systems (e.g., *E. coli*), enabling biochemical and immunological studies. Purified HupB is utilized to explore its DNA-binding properties, structural dynamics, and interactions with host immune components. Notably, HupB elicits immune responses in tuberculosis patients, suggesting its relevance in diagnostics or vaccine design. However, its exact role in pathogenesis remains under investigation, with conflicting evidence on its essentiality for Mtb survival.
Research on HupB recombinant protein continues to shed light on bacterial chromatin organization and its implications for combating persistent infections like tuberculosis.
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