| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | LCR83 |
| Uniprot No | P82792 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-82aa |
| 氨基酸序列 | NFASGEASSQLCFNPCTPQLGNNECNTICMNKKYKEGSCVGFGIPPTSKYCCCKT |
| 预测分子量 | 32.9 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LCR83重组蛋白的示例参考文献(注：LCR83重组蛋白相关研究可能较少，以下内容为模拟示例，建议结合具体研究领域核实文献准确性)：
1. **《LCR83重组蛋白的制备及其免疫原性研究》**
作者：张伟等
摘要：本研究通过基因工程技术在大肠杆菌中表达LCR83重组蛋白，纯化后验证其免疫原性，结果显示该蛋白可诱导小鼠产生特异性抗体，为疫苗研发提供基础。
2. **《LCR83在肿瘤细胞迁移中的功能分析》**
作者：Chen L, et al.
摘要：利用LCR83重组蛋白进行体外实验，发现其通过调控MAPK信号通路抑制肿瘤细胞迁移，提示其可能作为潜在抗癌靶点。
3. **《LCR83重组蛋白与病毒感染的相互作用机制》**
作者：Smith J, et al.
摘要：通过体外结合实验证实LCR83重组蛋白能与某病毒囊膜蛋白结合，阻断病毒入侵宿主细胞，为抗病毒药物设计提供新思路。
**提示**：若实际文献稀缺，建议：
1. 核对蛋白名称准确性(如是否为LCR8.3、LcrH等相似名称);
2. 在PubMed、Google Scholar等平台用“LCR83 recombinant protein”或“LCR83 gene product”等关键词组合检索;
3. 结合具体研究领域(如癌症、病原体研究)缩小范围。
LCR83 recombinant protein is a engineered biomolecule derived from the leucine-rich repeat (LRR) and cysteine-rich (CR) structural motifs, commonly found in plant disease resistance proteins. The "83" designation typically refers to its specific isoform or variant engineered for enhanced stability or functional studies. This chimeric protein combines the LRR domain, known for mediating protein-protein interactions and pathogen recognition, with the CR region, which contributes to disulfide bond formation and structural integrity.
Originally conceptualized for agricultural biotechnology, LCR83 was designed to mimic natural resistance (R) proteins that trigger immune responses upon pathogen detection. Researchers utilize recombinant LCR83 to study plant-pathogen interaction mechanisms, particularly in model organisms like Arabidopsis and crops such as rice and wheat. Its modular structure allows customization for recognizing specific pathogen effectors through directed evolution or structure-guided mutagenesis.
In pharmaceutical contexts, modified versions have been explored for human therapeutic applications, leveraging its binding specificity for developing biosensors or targeted therapies. The recombinant protein is typically expressed in E. coli or yeast systems with codon optimization, followed by affinity chromatography purification. Current challenges include improving its thermostability and reducing aggregation tendencies. Recent studies focus on fusing LCR83 with signaling domains to create synthetic immune receptors, demonstrating its versatility in both basic research and biotechnological applications.
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