纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | L |
Uniprot No | Q9H9P8 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 52-463aa |
氨基酸序列 | VIVGGGIVGLASARALILRHPSLSIGVLEKEKDLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALLYEYCQQKGISYKQCGKLIVAVEQEEIPRLQALYEKGLQNGVPGLRLIQQEDIKKKEPYCRGLMAIDCPHTGIVDYRQVALSFAQDFQEAGGSVLTNFEVKGIEMAKESPSRSIDGMQYPIVIKNTKGEEIRCQYVVTCAGLYSDRISELSGCTPDPRIVPFRGDYLLLKPEKCYLVKGNIYPVPDSRFPFLGVHFTPRMDGSIWLGPNAVLAFKREGYRPFDFSATDVMDIIINSGLIKLASQNFSYGVTEMYKACFLGATVKYLQKFIPEITISDILRGPAGVRAQALDRDGNLVEDFVFDAGVGDIGNRILHVRNAPSPAATSSIAISGMIADEVQQRFEL |
预测分子量 | 61.3kDa |
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“L重组蛋白”的示例参考文献(注:部分文献为示例性描述,实际引用时请核实真实性和准确性):
---
1. **文献名称**: *Expression and Functional Analysis of Recombinant L Protein from Vesicular Stomatitis Virus*
**作者**: Zhang Y, et al.
**摘要**: 本研究在大肠杆菌中成功表达了水疱性口炎病毒(VSV)的L蛋白,并验证了其RNA依赖的RNA聚合酶活性,为抗病毒药物开发提供了实验基础。
2. **文献名称**: *Cryo-EM Structure of the Lassa Virus L Protein in Complex with RNA*
**作者**: Li H, et al.
**摘要**: 通过昆虫细胞系统重组表达拉沙病毒L蛋白,结合冷冻电镜技术解析了其与病毒RNA复合物的高分辨率结构,阐明了其催化机制和潜在药物结合位点。
3. **文献名称**: *Development of a Recombinant L-Protein-Based Vaccine for Rabies*
**作者**: Kumar S, Patel R.
**摘要**: 利用哺乳动物细胞表达系统制备重组狂犬病毒L蛋白,评估其作为亚单位疫苗的免疫原性,结果显示可诱导小鼠产生中和抗体。
4. **文献名称**: *High-Yield Purification of Recombinant L Protein from Hepatitis C Virus Using Affinity Chromatography*
**作者**: Tanaka M, et al.
**摘要**: 优化了丙型肝炎病毒L蛋白的重组表达条件,开发了一种基于镍柱亲和层析的高效纯化方案,为功能研究提供高纯度蛋白。
---
**注意**:以上文献为示例,实际研究中建议通过数据库(如PubMed、Google Scholar)以关键词“recombinant L protein”或“L protein expression”检索最新文献。若“L蛋白”特指某病毒或物种,需补充更具体的关键词(如“Lassa virus L protein”)。
**Background of L-Recombinant Proteins**
Recombinant proteins, engineered through genetic recombination technology, are produced by inserting target DNA sequences into host organisms (e.g., bacteria, yeast, or mammalian cells) to express specific proteins. The "L-recombinant protein" designation may refer to a protein variant or a specific class of recombinant proteins, often linked to viral or bacterial systems. For instance, in virology, the L-protein (large protein) is a critical component in viruses like rabies or vesicular stomatitis virus (VSV), functioning as an RNA-dependent RNA polymerase essential for viral replication.
The development of recombinant protein technology emerged in the 1970s, propelled by breakthroughs in molecular cloning and gene expression systems. Key milestones include the production of human insulin in *E. coli* (1982), which revolutionized therapeutic protein manufacturing. Recombinant proteins are now pivotal in therapeutics (e.g., monoclonal antibodies, vaccines), diagnostics, and research tools.
L-recombinant proteins, depending on their context, may be engineered for enhanced stability, activity, or scalability. Their production often involves optimizing codon usage, selecting appropriate expression hosts, and refining purification protocols (e.g., affinity chromatography). Challenges include minimizing post-translational modification discrepancies between host and native organisms and ensuring proper folding.
In biomedical research, L-recombinant proteins are utilized to study viral mechanisms, develop antiviral drugs, or design subunit vaccines. For example, the VSV L-protein has been a model for understanding RNA polymerase structures, aiding in broad-spectrum antiviral discovery. Industrial applications extend to biocatalysts and bioengineering, where tailored enzymes improve biochemical processes.
Advancements in synthetic biology and CRISPR-based editing continue to refine recombinant protein platforms, enabling precise customization of L-proteins for therapeutic efficacy or industrial robustness. This technology remains central to addressing global health challenges, including pandemic preparedness and personalized medicine.
×