| 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)：
---
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)。
---
**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.
×
