| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | hld |
| Uniprot No | P0A0M1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-26aa |
| 氨基酸序列 | MAQDIISTIGDLVKWIIDTVNKFTKK |
| 预测分子量 | 18.3 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HLD重组蛋白的示例参考文献(注：以下内容为模拟虚构，仅供参考)：
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1. **标题**: *High-yield expression and purification of HLD recombinant protein in E. coli*
**作者**: Zhang, L.; Wang, H.; Chen, J.
**摘要**: 本研究报道了利用大肠杆菌表达系统高效表达HLD重组蛋白的优化策略。通过密码子优化和诱导条件调控，蛋白产量达到120 mg/L。纯化后的HLD蛋白在体外实验中显示出显著的酶活性，为工业化生产奠定了基础。
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2. **标题**: *Structural characterization of HLD recombinant protein by X-ray crystallography*
**作者**: Smith, K.; Johnson, R.; Tanaka, M.
**摘要**: 通过X射线晶体学解析了HLD重组蛋白的三维结构(分辨率2.1 Å)，揭示了其活性位点的关键氨基酸残基。该研究为理解HLD的催化机制及基于结构的药物设计提供了重要依据。
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3. **标题**: *Functional analysis of HLD recombinant protein in a neurodegenerative disease model*
**作者**: Kumar, S.; Lee, Y.; Rossi, F.
**摘要**: 在小鼠神经退行性疾病模型中，HLD重组蛋白通过静脉注射显著减轻了病理标志物(如β-淀粉样蛋白)的沉积，并改善了认知功能。研究表明HLD可能通过调节蛋白错误折叠途径发挥作用。
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4. **标题**: *Comparison of eukaryotic vs. prokaryotic systems for HLD recombinant protein production*
**作者**: García, M.; Nguyen, T.; Müller, P.
**摘要**: 对比了毕赤酵母(真核)和大肠杆菌(原核)系统表达HLD重组蛋白的效率。结果显示，真核系统产生的蛋白糖基化修饰更接近天然形式，但原核系统的成本效益更高。
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**建议**：实际文献需通过PubMed、Web of Science或Google Scholar以关键词“HLD recombinant protein”或“HLD protein expression”检索。
**Background of HLD Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biotechnology and medicine. Among these, HLD (Hybrid Lytic Domain) recombinant proteins represent a novel class designed to enhance functionality by combining distinct structural or catalytic domains from natural proteins. Typically derived from bacteriophage-derived endolysins or other lytic enzymes, HLD proteins are optimized for targeted antimicrobial activity, biodegradation, or industrial biocatalysis.
The development of HLD proteins stems from advances in recombinant DNA technology, enabling precise domain fusion to achieve synergistic effects. For instance, integrating cell wall-binding domains with catalytic domains (e.g., peptidoglycan hydrolases) enhances specificity and efficiency in lysing bacterial pathogens, making them promising alternatives to traditional antibiotics. Such designs address rising antimicrobial resistance (AMR) by targeting conserved bacterial structures while minimizing off-target effects.
Beyond antimicrobial applications, HLD proteins are adapted for environmental and industrial uses. Engineered variants can degrade complex biopolymers (e.g., cellulose, plastics) or detoxify pollutants, aligning with sustainable biomanufacturing and bioremediation goals. Their modular design allows customization for stability, solubility, and activity under diverse conditions, facilitated by heterologous expression systems like *E. coli*, yeast, or cell-free platforms.
Recent research focuses on optimizing HLD protein production, structure-function relationships, and delivery mechanisms (e.g., encapsulation, conjugation). Challenges include scaling production cost-effectively, ensuring long-term stability, and navigating regulatory pathways for clinical or commercial use. Collaborations across synthetic biology, computational modeling, and AI-driven design accelerate innovation, positioning HLD recombinant proteins as versatile tools in addressing global health, industrial, and environmental challenges.
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