| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MVP |
| Uniprot No | Q14764 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-893aa |
| 氨基酸序列 | MATEEFIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPMRMVTVPPRHYCTVANPVSRDAQGLVLFDVTGQVRLRHADLEIRLAQDPFPLYPGEVLEKDITPLQVVLPNTALHLKALLDFEDKDGDKVVAGDEWLFEGPGTYIPRKEVEVVEIIQATIIRQNQALRLRARKECWDRDGKERVTGEEWLVTTVGAYLPAVFEEVLDLVDAVILTEKTALHLRARRNFRDFRGVSRRTGEEWLVTVQDTEAHVPDVHEEVLGVVPITTLGPHNYCVILDPVGPDGKNQLGQKRVVKGEKSFFLQPGEQLEQGIQDVYVLSEQQGLLLRALQPLEEGEDEEKVSHQAGDHWLIRGPLEYVPSAKVEVVEERQAIPLDENEGIYVQDVKTGKVRAVIGSTYMLTQDEVLWEKELPPGVEELLNKGQDPLADRGEKDTAKSLQPLAPRNKTRVVSYRVPHNAAVQVYDYREKRARVVFGPELVSLGPEEQFTVLSLSAGRPKRPHARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVNDRKDPQETAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARIIRTAVFGFETSEAKGPDGMALPRPRDQAVFPQNGLVVSSVDVQSVEPVDQRTRDALQRSVQLAIEITTNSQEAAAKHEAQRLEQEARGRLERQKILDQSEAEKARKELLELEALSMAVESTGTAKAEAESRAEAARIEGEGSVLQAKLKAQALAIETEAELQRVQKVRELELVYARAQLELEVSKAQQLAEVEVKKFKQMTEAIGPSTIRDLAVAGPEMQVKLLQSLGLKSTLITDGSTPINLFNTAFGLLGMGPEGQPLGRRVASGPSPGEGISPQSAQAPQAPGDNHVVPVLR |
| 预测分子量 | 99,3 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3-4条关于MVP(Major Vault Protein)重组蛋白的虚构参考文献示例(仅供参考，实际文献需查阅数据库如PubMed等)：
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1. **标题**: *Structural Insights into MVP Recombinant Protein Assembly*
**作者**: Smith J, et al.
**摘要**: 通过冷冻电镜技术解析了重组MVP蛋白的自组装机制，发现其形成穹窿样纳米颗粒的关键结构域，为设计靶向药物载体提供了分子基础。
2. **标题**: *Recombinant MVP as a Drug Delivery Vehicle: In Vitro and In Vivo Evaluation*
**作者**: Lee H, et al.
**摘要**: 利用重组MVP蛋白包载化疗药物阿霉素，验证了其在体外细胞模型和小鼠肿瘤模型中增强药物递送效率并降低毒性的潜力。
3. **标题**: *Functional Interaction Between Recombinant MVP and Cellular Transport Proteins*
**作者**: Garcia R, et al.
**摘要**: 揭示了重组MVP蛋白与细胞内膜转运蛋白(如ABC转运体)的相互作用，表明其在多药耐药性(MDR)中的调控作用。
4. **标题**: *Engineering Thermostable MVP Recombinant Variants for Biomedical Applications*
**作者**: Wang Y, et al.
**摘要**: 通过定向进化技术开发了热稳定性增强的重组MVP突变体，拓展了其在高温环境下的应用场景(如疫苗佐剂或诊断试剂)。
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**备注**：以上文献为示例，实际研究需结合具体领域数据库(如NCBI、ScienceDirect)检索真实发表的文章。
**Background of MVP Recombinant Protein**
The Major Vault Protein (MVP), also known as the Lung Resistance-Related Protein (LRP), is the primary structural component of vault particles, which are evolutionarily conserved ribonucleoprotein complexes found in eukaryotic cells. Vaults are large, barrel-shaped organelles with a hollow interior, and MVP constitutes over 70% of their total mass. First identified in the 1980s, vaults are implicated in diverse cellular processes, including intracellular transport, multidrug resistance, and innate immunity, though their precise biological functions remain under investigation.
MVP is a 100-kDa protein characterized by repetitive structural domains that facilitate self-assembly into the vault’s distinctive architecture. Its ability to form stable, symmetrical complexes makes it a unique subject for structural biology and nanotechnology research. Recombinant MVP technology involves expressing the MVP gene in heterologous systems (e.g., bacteria, insect cells, or mammalian cells) to produce purified, functional protein for experimental or therapeutic applications. This approach bypasses the challenges of isolating MVP from natural sources, enabling scalable production and engineering of modified variants.
Recombinant MVP has gained attention for its potential in drug delivery and biomedical engineering. The vault particle’s hollow structure and biocompatibility suggest utility as a nanocontainer for encapsulating therapeutic molecules, such as chemotherapeutics, proteins, or nucleic acids. Additionally, MVP’s role in cellular resistance mechanisms has spurred studies on its involvement in cancer progression and response to treatment. Researchers also explore MVP-based vaccines, leveraging its capacity to carry antigens and stimulate immune responses.
Current research focuses on optimizing MVP expression systems, understanding its interaction with other vault components (e.g., non-coding RNAs), and clarifying its physiological roles in health and disease. As a modular platform, recombinant MVP bridges nanotechnology and biomedicine, offering innovative solutions for targeted therapies and diagnostic tools.
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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