| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GML |
| Uniprot No | Q99445 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-158aa |
| 氨基酸序列 | SAT MRAQWTYSLR CHDCAVINDF NCPNIRVCPY HIRRCMTISI RINSRELLVY KNCTNNCTFV YAAEQPPEAP GKIFKTNSFY WVCCCNSMVC NAGGPTNLER DMLPDEVTEE ELPEGTVRLG VSKLLLSFAS IIVSNILP |
| 预测分子量 | 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GML(甘油单月桂酸酯)重组蛋白的参考文献示例(注：文献信息为模拟虚构，仅供参考格式)：
---
1. **文献名称**: *Enhanced Expression of Recombinant Proteins Using GML-Based Fermentation Systems*
**作者**: Smith J, et al.
**摘要**: 研究探讨了在细菌发酵过程中添加GML对重组蛋白表达效率的影响，发现GML可通过调节细胞膜通透性提高目标蛋白产量，并减少包涵体形成。
2. **文献名称**: *Antimicrobial Activity of GML-Fused Lysozyme Recombinant Protein*
**作者**: Chen L, et al.
**摘要**: 报道了一种将GML与溶菌酶融合表达的重组蛋白，实验表明该蛋白对金黄色葡萄球菌具有显著抑菌作用，可能源于GML破坏细菌膜结构与溶菌酶的协同效应。
3. **文献名称**: *GML as a Novel Adjuvant for Recombinant Vaccine Development*
**作者**: Gupta R, et al.
**摘要**: 评估了GML作为疫苗佐剂与重组抗原蛋白联用的效果，证明其能增强小鼠模型中的Th1型免疫应答，为新型佐剂设计提供了理论依据。
---
**说明**：以上文献为示例性内容，实际研究中请通过PubMed、Google Scholar等平台检索真实文献(关键词：GML recombinant protein, glyceryl laurate, protein expression, antimicrobial adjuvant)。
**Background of GML Recombinant Protein**
Recombinant protein technology has revolutionized biomedical research and therapeutic development by enabling the production of tailored proteins through genetic engineering. GML (Glycosylphosphatidylinositol-Anchored Metalloproteinase-Like Protein) recombinant protein is a synthetic or engineered version of naturally occurring proteins, designed to mimic specific biological functions or enhance stability and activity. This technology involves inserting the gene encoding the target protein into a host organism (e.g., bacteria, yeast, or mammalian cells), which then expresses the protein in large quantities.
GML proteins, in particular, are of interest due to their structural and functional roles in cellular processes, such as cell adhesion, signaling, and enzymatic activity. Their recombinant forms are often optimized for applications in drug development, diagnostics, and vaccine production. For example, GML recombinant proteins may serve as antigens for antibody generation, tools for studying protein-protein interactions, or components in biotherapeutics targeting cancers or infectious diseases.
The production of GML recombinant proteins leverages advancements in molecular cloning, fermentation, and purification techniques. Key challenges include maintaining proper post-translational modifications (e.g., glycosylation) and ensuring conformational integrity, which are critical for biological activity. Mammalian expression systems are often preferred for complex proteins requiring human-like modifications.
In recent years, GML recombinant proteins have gained traction in personalized medicine and biopharmaceuticals due to their specificity, scalability, and reduced immunogenicity compared to traditional therapeutics. Ongoing research focuses on improving yield, cost-effectiveness, and functional fidelity, positioning recombinant proteins like GML as pivotal tools in modern biotechnology and medicine.
×
