| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LZM |
| 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 | 30.7kDa |
| 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LZM(溶菌酶)重组蛋白的3篇代表性文献摘要(部分信息为模拟示例)：
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1. **文献名称**：Expression and purification of recombinant human lysozyme in Pichia pastoris
**作者**：Zhang L. et al.
**摘要**：本研究利用毕赤酵母表达系统成功实现重组人溶菌酶的高效分泌表达，通过优化甲醇诱导条件和培养基成分，使酶活性达到1200 U/mg。纯化产物在体外抑菌实验中显著抑制金黄色葡萄球菌生长，为规模化生产医用溶菌酶提供参考。
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2. **文献名称**：Enhancing thermostability of recombinant lysozyme through site-directed mutagenesis
**作者**：Wang Y., Chen H.
**摘要**：通过分子动力学模拟筛选溶菌酶热敏感位点，构建T26P/K33R双突变体重组蛋白。突变体在65℃下的半衰期延长至野生型的3倍，同时保持原有溶菌活性，为食品工业高温加工环境中的应用奠定基础。
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3. **文献名称**：Bacillus subtilis as a novel host for economical lysozyme production
**作者**：Kim S.J., et al.
**摘要**：开发基于枯草芽孢杆菌的重组溶菌酶表达系统，利用自溶特性简化下游纯化流程。发酵72小时后产量达2.8 g/L，成本较传统大肠杆菌体系降低40%，且产物天然无内毒素污染。
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注：以上内容为学术文献模拟示例，实际文献需通过PubMed、Web of Science等数据库检索获取。建议结合关键词"recombinant lysozyme"、"heterologous expression"、"antimicrobial activity"进行扩展检索。
LZM recombinant protein, typically referring to recombinant lysozyme, is a bioengineered version of the naturally occurring enzyme lysozyme, which plays a critical role in innate immunity by breaking down bacterial cell walls. Originally discovered in 1921 by Alexander Fleming, lysozyme is a muramidase that hydrolyzes β-1.4-glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, a key structural component of Gram-positive bacterial walls. While natural lysozyme is widely sourced from egg whites (hen egg-white lysozyme, HEWL) or human secretions, recombinant technology enables its production in heterologous expression systems like *E. coli*, yeast, or mammalian cells, ensuring higher purity, scalability, and reduced allergenicity.
The development of LZM recombinant protein stems from the need for cost-effective, sustainable, and customizable alternatives to traditional extraction methods. Recombinant variants can be engineered for enhanced stability, altered substrate specificity, or reduced immunogenicity, broadening their applications. For instance, thermostable lysozymes are valuable in food preservation, while modified versions are explored for antimicrobial therapies, particularly against antibiotic-resistant pathogens. Additionally, recombinant lysozyme serves as a model protein in structural biology and drug delivery studies due to its well-characterized properties.
Recent advancements focus on fusion proteins combining lysozyme with other antimicrobial agents or targeting motifs, aiming to improve therapeutic efficacy. Despite challenges in expression yield and folding efficiency, LZM recombinant proteins hold promise in pharmaceuticals, biotechnology, and industrial processes, aligning with global trends toward precision medicine and green chemistry. Ongoing research continues to optimize production platforms and explore novel functionalities, reinforcing its role as a versatile tool in science and industry.
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