| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | nisZ |
| Uniprot No | P29559 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-57aa |
| 氨基酸序列 | MSTKDFNLDLVSVSKKDSGASPRITSISLCTPGCKTGALMGCNMKTATCNCSIHVSK |
| 预测分子量 | 5.9kDa |
| 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nisZ重组蛋白的3篇文献信息：
1. **《Genetic engineering of nisin Z production by Lactococcus lactis》**
- 作者：Kuipers, O.P. 等
- 摘要：研究通过基因重组技术在乳酸乳球菌中优化nisZ(nisin Z变体)的生物合成，通过启动子调控和基因拷贝数调整提高产量，并验证其抑菌活性。
2. **《Heterologous expression and characterization of nisin Z in Escherichia coli》**
- 作者：Liu, X. 等
- 摘要：报道利用大肠杆菌表达系统生产重组nisZ蛋白，通过融合标签纯化并复性，证明其对革兰氏阳性菌的抑制效果，为规模化生产提供新策略。
3. **《Enhanced production of recombinant nisin Z in Pichia pastoris》**
- 作者：van der Meer, J.R. 等
- 摘要：在毕赤酵母中实现nisZ的高效分泌表达，通过发酵条件优化使产量显著提升，并验证其在食品防腐中的潜在应用。
注：上述文献为示例，实际检索时需通过学术数据库(如PubMed、Web of Science)确认具体细节及可用性。
**Background of NisZ Recombinant Protein**
NisZ, a variant of the lantibiotic nisin, is a bacteriocin produced by certain *Lactococcus lactis* strains. Nisin, widely recognized for its potent antimicrobial activity against Gram-positive bacteria, has been extensively studied and utilized as a natural food preservative. NisZ differs from the prototypical nisin A by a single amino acid substitution (asparagine to histidine at position 27), which slightly alters its physicochemical properties and antimicrobial spectrum. This modification enhances its stability under specific conditions, making it a candidate for applications in diverse environments.
The production of recombinant NisZ leverages genetic engineering to express the *nisZ* gene in heterologous hosts, such as *Escherichia coli* or yeast, bypassing the limitations of native bacterial fermentation. Recombinant technology allows for scalable production, improved purity, and the potential for further protein engineering. The biosynthesis involves post-translational modifications, including dehydration of serine/threonine residues and formation of thioether bridges (lanthionine rings), critical for its bioactive conformation.
NisZ’s mechanism involves binding to lipid II, a key bacterial cell wall precursor, disrupting cell wall synthesis and forming pores in membranes. Its activity against antibiotic-resistant pathogens, including methicillin-resistant *Staphylococcus aureus* (MRSA), has spurred interest in therapeutic applications. Additionally, its low toxicity to mammalian cells and biodegradability align with sustainable and safe use in food and healthcare.
Research continues to optimize expression systems, enhance stability, and explore hybrid variants combining NisZ’s traits with other functional domains. Challenges include maintaining bioactivity in recombinant hosts and ensuring cost-effective production. Despite these hurdles, NisZ represents a promising alternative in the fight against antimicrobial resistance and spoilage microbes, bridging traditional bacteriocin biology with modern biotechnological innovation.
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