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):
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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。
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**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.
在生物科技领域,蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者,凭借自身卓越的研发实力,每年能成功研发 1000 多种全新蛋白,在重组蛋白领域不断突破。 在重组蛋白生产过程中,艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白,到具有特定催化功能的酶、参与信号传导的激酶,再到用于免疫研究的病毒抗原,艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统,昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势,能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求,从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品,更是从源头到终端的一站式解决方案。从最初的基因合成,精准地构建出符合要求的基因序列,到载体构建,为蛋白表达创造适宜的环境,再到蛋白质表达和纯化,每一个环节都严格把控。我们充分尊重客户的个性化需求,在表达 / 纯化标签的选择、表达宿主的确定等方面,为客户量身定制专属方案。 同时,艾普蒂还配备了多种纯化体系,能够应对不同特性蛋白的纯化需求。这种灵活性和专业性,极大地提高了蛋白表达和纯化的成功率,让客户的研究项目得以顺利推进,在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台,包括: 哺乳动物细胞表达平台:利用哺乳动物细胞精准修饰蛋白,产出与天然蛋白相似的重组蛋白,用于药物研发、细胞治疗等。 杂交瘤开发平台:通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株,优化后的技术让抗体亲和力与特异性更高,应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台:FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞;Beacon® 基于微流控技术,单细胞水平捕获、分析 B 细胞,挖掘抗体多样性,缩短开发周期。 凭借这些平台,艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务,推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富,拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上,艾普蒂生物不仅经验老到,还积累了详实的成功案例。针对客户的工业化生产需求,我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节,对重组蛋白基因序列进行优化,全面探索多种条件,精准找出最契合客户需求的生产方法。 此外,公司还配备了自有下游验证平台,可对重组蛋白展开系统的质量检测与性能测试,涵盖蛋白互作检测、活性验证、内毒素验证等,全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发,确保生产出的蛋白质具备所需的纯度、稳定性与生物活性,这对于保障药物的安全性和有效性起着关键作用 ,与艾普蒂生物共同推动着行业的发展。
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