| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VMO1 |
| Uniprot No | Q7Z5L0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-202aa |
| 氨基酸序列 | QTDGRNGYTAVIEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGIPG DDTALNGIRLHCARGNVLGNTHVVESQSGSWGEWSEPLWCRGGAYLVAFS LRVEAPTTLGDNTAANNVRFRCSDGEELQGPGLSWGDFGDWSDHCPKGAC GLQTKIQGPRGLGDDTALNDARLFCCRSVDHHHHHH |
| 预测分子量 | 20 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VMO1重组蛋白的模拟参考文献示例(注：部分文献信息为示例性概括，实际文献需通过学术数据库验证)：
---
1. **文献名称**: "Molecular cloning and recombinant expression of avian VMO1: a structural protein of the vitelline membrane"
**作者**: Kodama, T., et al.
**摘要**: 本研究报道了鸡VMO1基因的克隆及其在大肠杆菌中的重组表达。通过体外纯化获得重组VMO1蛋白，并证实其在体外具有抑制革兰氏阴性菌生长的抗菌活性，提示其可能在卵的先天免疫中发挥作用。
2. **文献名称**: "Functional characterization of recombinant VMO1 in oocyte-sperm interaction"
**作者**: Smith, J.L., & Johnson, R.K.
**摘要**: 利用昆虫细胞系统表达重组VMO1蛋白，探究其与精子表面蛋白的相互作用。实验表明，VMO1可能通过介导配子结合参与受精过程，为生殖生物学研究提供新方向。
3. **文献名称**: "Structural analysis of VMO1 recombinant protein using X-ray crystallography"
**作者**: Zhang, Y., et al.
**摘要**: 通过重组表达技术获得高纯度VMO1蛋白，并解析其晶体结构。结构分析揭示了VMO1独特的β-折叠构象，为理解其机械支撑及酶结合功能提供分子基础。
4. **文献名称**: "Optimization of VMO1 expression in Pichia pastoris for industrial applications"
**作者**: Tanaka, H., et al.
**摘要**: 研究优化了毕赤酵母系统中重组VMO1的高效表达工艺，评估其作为生物材料(如可降解膜)的潜力，证明其热稳定性和可塑性适用于生物技术领域。
---
**建议**：以上内容为基于领域知识的示例，实际文献需通过PubMed、Google Scholar等平台以关键词“VMO1 recombinant protein”或“VMO1 expression”检索，并筛选近年研究以获取准确信息。
**Background of VMO1 Recombinant Protein**
VMO1 (Vitelline Membrane Outer Layer Protein 1) is a protein initially identified in avian species, where it plays a structural and functional role in the formation and stabilization of the vitelline membrane, a critical extracellular matrix surrounding the egg yolk. This membrane is essential for embryonic development, providing mechanical protection and regulating nutrient exchange. VMO1 is characterized by its cysteine-rich domains, which contribute to disulfide bond formation, ensuring structural integrity under physiological conditions.
The recombinant form of VMO1 is produced using genetic engineering techniques, often expressed in prokaryotic (e.g., *E. coli*) or eukaryotic (e.g., yeast, mammalian cells) systems to achieve proper folding and post-translational modifications. Recombinant VMO1 retains the functional properties of the native protein, enabling researchers to study its interactions with other biomolecules, such as zona pellucida proteins in mammalian oocytes, and its potential involvement in fertility-related processes.
Recent studies suggest that VMO1 may have broader biological significance beyond avian reproduction. It has been detected in mammalian tissues, including the liver and kidneys, hinting at roles in cellular adhesion, immune response modulation, or tissue remodeling. Its conserved domains across species also imply evolutionary importance. Recombinant VMO1 serves as a valuable tool for investigating these mechanisms, aiding in the development of biomedical applications, such as fertility treatments, contraceptives, or biomaterials inspired by its resilient structural properties.
Ongoing research aims to elucidate its molecular pathways and therapeutic potential, positioning VMO1 as a protein of interest in both developmental biology and applied biotechnology.
×
