| 纯度 | >90%SDS-PAGE. |
| 种属 | Chicken |
| 靶点 | VTG2 |
| Uniprot No | P02845 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-653aa |
| 氨基酸序列 | SRRSYLYNYEGSMLNGLQDRSLGKAGVRLSSKLEISGLPENAYLLKVRSPQVEEYNGVWPRDPFTRSSKITQVISSCFTRLFKFEYSSGRIGNIYAPEDCPDLCVNIVRGILNMFQMTIKKSQNVYELQEAGIGGICHARYVIQEDRKNSRIYVTRTVDLNNCQEKVQKSIGMAYIYPCPVDVMKERLTKGTTAFSYKLKQSDSGTLITDVSSRQVYQISPFNEPTGVAVMEARQQLTLVEVRSERGSAPDVPMQNYGSLRYRFPAVLPQMPLQLIKTKNPEQRIVETLQHIVLNNQQDFHDDVSYRFLEVVQLCRIANADNLESIWRQVSDKPRYRRWLLSAVSASGTTETLKFLKNRIRNDDLNYIQTLLTVSLTLHLLQADEHTLPIAADLMTSSRIQKNPVLQQVACLGYSSVVNRYCSQTSACPKEALQPIHDLADEAISRGREDKMKLALKCIGNMGEPASLKRILKFLPISSSSAADIPVHIQIDAITALKKIAWKDPKTVQGYLIQILADQSLPPEVRMMACAVIFETRPALALITTIANVAMKESNMQVASFVYSHMKSLSKSRLPFMYNISSACNIALKLLSPKLDSMSYRYSKVIRADTYFDNYRVGATGEIFVVNS |
| 预测分子量 | 74.9kDa |
| 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VTG2重组蛋白的3篇模拟参考文献(注：内容为虚构，仅作示例)：
1. **文献名称**: *Expression and purification of recombinant VTG2 in zebrafish for environmental estrogen detection*
**作者**: Chen L, Wang Y, Zhang H.
**摘要**: 本研究通过克隆斑马鱼VTG2基因至大肠杆菌表达系统，成功表达并纯化了重组VTG2蛋白。实验证明该蛋白可用于水体中环境雌激素(如双酚A)的生物标志物检测，灵敏度显著提高。
2. **文献名称**: *Functional characterization of honeybee VTG2 in immune response regulation*
**作者**: Müller S, Schmidt J.
**摘要**: 利用杆状病毒-昆虫细胞系统表达蜜蜂VTG2重组蛋白，发现其不仅参与卵黄形成，还在工蜂免疫应答中调控抗菌肽表达，为昆虫生殖与免疫交叉机制提供新证据。
3. **文献名称**: *Structural comparison of recombinant VTG2 isoforms across teleost species*
**作者**: Kim T, Tanaka M, Lee S.
**摘要**: 通过毕赤酵母表达系统制备了鲑鱼、青鳉和罗非鱼的VTG2重组蛋白，并利用X射线晶体学分析其结构差异，揭示了不同鱼类卵黄蛋白原在脂质结合能力上的进化适应性。
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提示：实际文献需通过数据库(如PubMed、Web of Science)以关键词“VTG2 recombinant”“vitellogenin 2 expression”检索，部分真实研究可能集中于水生生物毒性测试或生殖内分泌学领域。
**Background of VTG2 Recombinant Protein**
Vitellogenin (VTG) is a large glycolipophosphoprotein precursor crucial for yolk formation in oviparous (egg-laying) vertebrates and invertebrates. It is synthesized primarily in the liver (or analogous tissues) under estrogenic regulation and transported to developing oocytes, where it is cleaved into yolk proteins to support embryonic growth. VTG2. a specific isoform or homolog of vitellogenin, has been identified in various species, including fish, amphibians, and invertebrates, often differing in structural or functional properties from other VTG isoforms. For instance, in zebrafish (*Danio rerio*), *vtg2* is one of multiple vitellogenin genes, with its expression strongly induced by estrogenic stimuli, making it a biomarker for endocrine disruption studies.
Recombinant VTG2 refers to the protein produced via genetic engineering, typically by inserting the VTG2 gene into expression systems like *Escherichia coli*, yeast, or mammalian cells. This approach enables scalable, high-purity production of the protein without relying on native sources, which is particularly valuable given ethical and practical challenges in harvesting VTG from live organisms. Recombinant technology also allows for modifications, such as tagging (e.g., His-tags) to facilitate purification or detection.
The significance of VTG2 recombinant protein lies in its applications in environmental toxicology and reproductive biology. It serves as a sensitive biomarker in ecotoxicological assays to detect estrogen-mimicking pollutants (e.g., endocrine-disrupting chemicals) in water systems. Additionally, recombinant VTG2 aids in studying ovarian development, yolk metabolism, and evolutionary conservation of reproductive mechanisms. Its use in immunoassays (e.g., ELISA) or antibody development further supports standardized testing protocols.
Despite its utility, challenges persist, such as ensuring proper post-translational modifications (e.g., phosphorylation, glycosylation) in heterologous expression systems, which may affect functional accuracy. Ongoing research focuses on optimizing expression platforms and validating recombinant VTG2's bioactivity to enhance its reliability in both scientific and industrial contexts.
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