| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LPO |
| Uniprot No | P22079 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 81-712aa |
| 氨基酸序列 | TRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLEVGCGAPAPVV RCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTP GKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDF APDTELGSSEYSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRA GFVCPTPPYKSLAREQINALTSFLDASFVYSSEPSLASRLRNLSSPLGLM AVNQEVSDHGLPYLPYDSKKPSPCEFINTTARVPCFLAGDSRASEHILLA TSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAFVQIITFRDYL PILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDE NYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMM TGELRNKLFQPTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQT LEELNTVLKSKMLAKKLLGLYGTPDNIDIWIGAIAEPLVERGRVGPLLAC LLGKQFQQIRDGDRFWWENPGVFTNEQKDSLQKMSFSRLVCDNTRITKVP RDPFWANSYPYDFVDCSAIDKLDLSPWASVKN |
| 预测分子量 | 77 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LPO(乳过氧化物酶，Lactoperoxidase)重组蛋白的示例文献摘要(内容为虚构，仅作格式参考)：
1. **《重组乳过氧化物酶在大肠杆菌中的高效表达及活性分析》**
- 作者：Smith J, et al.
- 摘要：本研究通过优化大肠杆菌表达系统，成功实现LPO的重组表达，并通过亲和层析纯化获得高纯度蛋白。活性实验表明，重组LPO具有与天然酶相似的抗菌性能，为工业化生产提供了新策略。
2. **《基于毕赤酵母的LPO重组表达及其在食品保鲜中的应用》**
- 作者：Wang L, et al.
- 摘要：利用毕赤酵母表达系统分泌重组LPO，通过发酵条件优化使产量提升3倍。实验证明，该重组蛋白可有效抑制牛奶中病原菌生长，延长货架期，具有食品工业应用潜力。
3. **《乳过氧化物酶结构域功能解析：重组蛋白定点突变研究》**
- 作者：Zhang Y, et al.
- 摘要：通过定点突变技术研究LPO催化结构域的功能，发现第126位组氨酸对酶活性至关重要。重组突变体活性显著降低，为理解LPO作用机制提供了分子基础。
4. **《重组LPO与溶菌酶协同抗菌效应及其伤口敷料开发》**
- 作者：Kim S, et al.
- 摘要：将重组LPO与溶菌酶结合制备抗菌敷料，体外实验显示协同作用可杀灭99%的金黄色葡萄球菌。动物模型证实其加速伤口愈合效果，具备医药应用前景。
(注：以上文献为示例，实际研究需查询PubMed、Web of Science等数据库获取真实文献。)
**Background of Recombinant LPO (Lactoperoxidase) Protein**
Lactoperoxidase (LPO), a member of the peroxidase enzyme family, is naturally found in mammalian secretions such as milk, saliva, and tears. It plays a critical role in innate immunity by catalyzing the oxidation of thiocyanate (SCN⁻) and iodide (I⁻) into antimicrobial agents (e.g., hypothiocyanite), which inhibit bacterial growth and protect mucosal surfaces. This enzyme has drawn significant interest for its potential applications in biotechnology, pharmaceuticals, and food preservation.
Recombinant LPO (rLPO) is produced using genetic engineering techniques, where the LPO gene is inserted into expression systems like *E. coli*, yeast, or mammalian cell lines. Unlike native LPO, which is extracted from natural sources with low yield and high cost, recombinant production offers scalability, consistency, and reduced ethical concerns. However, challenges persist in achieving proper post-translational modifications (e.g., glycosylation) critical for enzyme stability and activity, often necessitating eukaryotic expression systems.
In research, rLPO is utilized to study its antimicrobial mechanisms, immune modulation, and potential therapeutic roles in treating infections or inflammatory diseases. Industrially, it is explored as a natural preservative in dairy products and cosmetics. Recent advances in protein engineering aim to enhance rLPO’s catalytic efficiency and stability under varying conditions, broadening its applicability. Despite progress, optimizing expression systems and ensuring cost-effective large-scale production remain key hurdles. Overall, rLPO represents a promising tool bridging biochemistry, medicine, and industry, with ongoing studies expanding its functional versatility.
×
