| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LYZ |
| Uniprot No | P61626 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-148aa |
| 氨基酸序列 | KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV |
| 预测分子量 | 27.8 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LYZ(溶菌酶)重组蛋白研究的模拟参考文献示例(内容为虚构，仅作格式参考)：
1. **文献名称**: "High-level expression and purification of recombinant human lysozyme in Escherichia coli"
**作者**: Zhang, L., et al.
**摘要**: 研究利用大肠杆菌表达系统高效表达重组人溶菌酶，优化诱导条件及纯化工艺，产物展现与天然溶菌酶相似的酶活性和抑菌效果。
2. **文献名称**: "Functional characterization of a novel recombinant lysozyme from marine bacteria with enhanced thermal stability"
**作者**: Chen, W., & Park, S. H.
**摘要**: 从海洋细菌中克隆新型溶菌酶基因，通过毕赤酵母系统重组表达，该酶在高温及高盐条件下保持活性，显示潜在工业应用价值。
3. **文献名称**: "Recombinant lysozyme-loaded nanoparticles for targeted drug delivery against Helicobacter pylori"
**作者**: Gupta, R., et al.
**摘要**: 开发负载重组溶菌酶的pH响应型纳米颗粒，体外实验证实其可靶向胃部酸性环境释放药物，显著抑制幽门螺杆菌生长。
4. **文献名称**: "Comparative analysis of plant-derived vs. prokaryotic recombinant lysozyme in poultry feed applications"
**作者**: Martínez, F., et al.
**摘要**: 对比烟草表达系统与原核系统生产的重组溶菌酶，评估两者作为饲料添加剂的抑菌性能及成本效益，提出植物表达体系的规模化潜力。
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注：以上文献为示例性内容，实际引用需以真实数据库(如PubMed、ScienceDirect)检索结果为准。
**Background of Recombinant LYZ (Lysozyme) Protein**
Lysozyme (LYZ), a naturally occurring enzyme with potent antimicrobial properties, is widely recognized for its ability to degrade bacterial cell walls by hydrolyzing the β-1.4-glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan. First discovered by Alexander Fleming in 1921. it is abundantly found in biological secretions such as tears, saliva, and egg whites, playing a critical role in innate immunity.
Traditional lysozyme production relies on extraction from natural sources, particularly hen egg whites, which poses challenges including low yield, allergenicity risks, and ethical concerns related to animal use. To address these limitations, recombinant DNA technology has emerged as a sustainable alternative. Recombinant LYZ is produced by inserting the lysozyme gene into expression systems like *Escherichia coli*, yeast (*Pichia pastoris*), or plant-based platforms, enabling scalable and cost-effective production with reduced allergenic potential.
The recombinant form retains the functional characteristics of native lysozyme, including broad-spectrum activity against Gram-positive bacteria, making it valuable in pharmaceuticals (e.g., antibacterial therapies), food preservation, and biotechnology applications. Recent advances have also explored engineered variants with enhanced stability, modified substrate specificity, or synergistic effects when combined with other antimicrobial agents.
Despite its promise, challenges persist in optimizing expression efficiency, ensuring proper post-translational modifications (critical for activity), and overcoming resistance mechanisms in pathogens. Ongoing research focuses on improving production systems, tailoring lysozyme for targeted applications, and exploring novel delivery mechanisms.
Overall, recombinant LYZ represents a convergence of biotechnology and industrial demand, offering a safer, customizable, and sustainable solution to meet global needs in healthcare, food safety, and beyond. Its development underscores the potential of protein engineering in advancing therapeutic and commercial biomolecules.
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