| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Vg |
| Uniprot No | P22004 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 382-513aa |
| 氨基酸序列 | QQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH |
| 预测分子量 | 18.9kDa |
| 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Vg(卵黄蛋白原)重组蛋白的3篇示例参考文献，内容基于典型研究方向概括：
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1. **文献名称**：*Expression and purification of recombinant zebrafish vitellogenin for environmental estrogen detection*
**作者**：Zhang et al., 2020
**摘要**：本研究利用大肠杆菌表达系统成功制备了重组斑马鱼Vg蛋白，并通过Western blot验证其免疫活性。实验表明，该蛋白可与环境中的雌激素类污染物(如双酚A)特异性结合，为开发水体雌激素生物传感器提供了基础材料。
2. **文献名称**：*Functional characterization of recombinant Bombyx mori vitellogenin in ovarian development*
**作者**：Li et al., 2018
**摘要**：通过杆状病毒-昆虫细胞系统表达家蚕Vg重组蛋白，发现其能够被卵巢细胞高效摄取并促进卵母细胞成熟。研究揭示了Vg在昆虫生殖周期中的关键作用，为靶向Vg的害虫防控策略提供了理论依据。
3. **文献名称**：*Recombinant Vg protein from Litopenaeus vannamei: production and its role in shrimp reproduction*
**作者**：Wang et al., 2021
**摘要**：采用真核表达系统制备凡纳滨对虾重组Vg蛋白，证实其与卵黄颗粒的结合能力，并证明外源添加Vg可显著提高雌虾产卵量。该研究为水产养殖中甲壳类繁殖调控技术开发提供了新思路。
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**注**：以上文献为示例，实际研究中请通过学术数据库(如PubMed、Web of Science)检索具体论文。如需进一步协助筛选真实文献，可提供更多关键词或研究背景。
**Background of Vg Recombinant Protein**
Vg (vitellogenin) is a large glycolipoprotein precursor of egg yolk proteins, primarily synthesized in the liver (or fat body in invertebrates) of oviparous animals under estrogenic regulation. It plays a critical role in reproductive biology by transporting nutrients to developing oocytes. Structurally, Vg contains conserved domains for lipid binding, cleavage sites for proteolytic processing into yolk proteins, and motifs involved in immune modulation.
The recombinant Vg protein is engineered through heterologous expression systems (e.g., *E. coli*, yeast, or insect cells*) to study its biological functions and applications. Recombinant technology allows large-scale production, enabling research on Vg’s roles beyond reproduction, including antioxidant activity, immune response regulation, and social behavior modulation in insects like honeybees.
In ecotoxicology, recombinant Vg serves as a biomarker for endocrine-disrupting chemicals (EDCs), as its synthesis is estrogen-sensitive. Its detection in male or juvenile organisms indicates environmental estrogenic exposure. Additionally, recombinant Vg has biotechnological potential in aquaculture and apiculture to enhance reproductive health or stress resilience.
Challenges in Vg recombinant production include its large size (>200 kDa), post-translational modifications (e.g., glycosylation), and solubility. Advanced expression systems, such as baculovirus-insect cell platforms, are often employed to address these issues.
Overall, recombinant Vg protein bridges fundamental research and applied sciences, offering insights into developmental biology, environmental monitoring, and sustainable agriculture. Its study continues to reveal evolutionary conserved mechanisms and novel applications in biomedicine and ecology.
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