| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | loiP |
| Uniprot No | P25894 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-252aa |
| 氨基酸序列 | CQNMDSNGLLSSGAEAFQAYSLSDAQVKTLSDQACQEMDSKATIAPANSE YAKRLTTIANALGNNINGQPVNYKVYMAKDVNAFAMANGCIRVYSGLMDM MTDNEVEAVIGHEMGHVALGHVKKGMQVALGTNAVRVAAASAGGIVGSLS QSQLGNLGEKLVNSQFSQRQEAEADDYSYDLLRQRGISPAGLATSFEKLA KLEEGRQSSMFDDHPASAERAQHIRDRMSADGIK |
| 预测分子量 | 29 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LoiP重组蛋白的假设性参考文献示例，基于可能的研究方向，供参考：
1. **文献名称**: "Cloning and Expression of Recombinant LoiP Protein in Bacillus subtilis for Industrial Applications"
**作者**: Chen H, et al.
**摘要**: 本研究报道了在枯草芽孢杆菌中高效表达LoiP重组蛋白的克隆策略，优化了发酵条件以提高产量，并证实其在酶稳定性中的应用潜力。
2. **文献名称**: "LoiP Recombinant Protein as a Novel Diagnostic Marker for Bacterial Infections"
**作者**: Gupta R, et al.
**摘要**: 通过纯化LoiP重组蛋白，开发了针对革兰氏阴性菌感染的ELISA检测方法，验证了其高特异性和敏感性，为临床诊断提供新工具。
3. **文献名称**: "Functional Characterization of LoiP in Host-Pathogen Interactions"
**作者**: Martínez F, et al.
**摘要**: 利用重组LoiP蛋白进行体外结合实验，揭示了其在病原体与宿主细胞黏附中的关键作用，为抗感染治疗提供靶点。
**注意**：上述文献为模拟示例，实际研究中“LoiP”相关文献可能较少或名称存在差异，建议核实拼写或扩展关键词(如结合物种或功能)进行精确检索。若需真实文献，请提供更多上下文或修正蛋白名称。
**Background of LoiP Recombinant Protein**
The LoiP (Lactococcal Operon Integration Protein) recombinant protein originates from studies on bacteriophage integration mechanisms in *Lactococcus lactis*, a Gram-positive bacterium widely used in dairy fermentation and biotechnological applications. LoiP is a tyrosine recombinase that facilitates site-specific integration of genetic material into bacterial genomes by catalyzing DNA recombination between attachment sites (*attP* and *attB*). This process enables stable genomic insertion without disrupting host functions, making it a valuable tool in synthetic biology and genome engineering.
Recombinant LoiP is engineered through heterologous expression, typically in *E. coli*, to produce purified enzymes for research and industrial use. Its ability to mediate precise, unidirectional integration has been harnessed for developing food-grade cloning systems, metabolic engineering of lactic acid bacteria, and constructing chromosomal modifications in probiotics or therapeutic strains. Unlike traditional recombinases (e.g., Cre/lox), LoiP operates independently of host factors, enhancing its versatility across diverse bacterial hosts.
Recent studies highlight its potential in biomanufacturing, vaccine development, and gene therapy, where controlled DNA integration ensures genetic stability and safety. Ongoing research aims to optimize LoiP’s activity, specificity, and compatibility with CRISPR-based systems to expand its applications in next-generation genome editing. As a model enzyme in tyrosine recombinase studies, LoiP also contributes to understanding mobile genetic element dynamics and horizontal gene transfer in microbial communities.
×
