| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GV51_0914 |
| Uniprot No | D6SZ78 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-525aa |
| 氨基酸序列 | MKDTFCSYYTNSDEITSYMVNRLEIEENDIILEPSAGEGIFIDQILNSNK MIQIDALDINAEAIKILNSKYQDLPSITVRETDTLLDERLDLLSSPELWI KQTDTLLDEQLNFFGSIGGHYNKVIGNPPYGAWQDYDKRAQLKKKYPGQY VKETYSLFLLRCISLLRNGGRLSFIIPDTYLFLNLHAKLRELLLTSTRII EIITFPSKFFPGVSFGYSNLSIITLERTNKENALNNTVRIVQGFESANEF QLLLNDSQLPDNLSTFFVKQSDVLTNDKHRFILADSSTNAIINTALIRLG DVANIVTGFYTGDNKRFIRAADDSVKGSKNYEKVNPSQIFNCSSLSGIKE VSEGYIPYVKSASKTRYYREKDEWFVRWDEDTIEYYNSHPKSRFQNSAFY FKKGVAIPMVKASTIRAFYIKNRVFDQSIVGIFPKDQSKILYVLALMNSD IVNELIHTINPTANNSANYIKQIPYFEPPKSVLEKINNKVKHILSLGEKG KITECEKLHSELNHTINELYSNFRK |
| 预测分子量 | 64 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. |
关于“GV51_0914重组蛋白”的公开文献目前无法在主流学术数据库(如PubMed、Web of Science等)中检索到，可能是以下原因导致：
1. **内部编号或未公开研究**：该名称可能是某实验室的内部项目编号，尚未发表或数据未公开。
2. **命名差异**：不同研究团队对同一蛋白可能使用不同命名规则(如GenBank编号或专利代码)，需更多背景信息辅助检索。
3. **新兴领域研究**：若涉及最新技术(如mRNA疫苗载体蛋白或新型病毒抗原)，可能处于预印本或专利阶段，尚未收录。
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### 建议解决方案：
1. **核对名称准确性**：确认“GV51_0914”是否为正确编号或存在拼写变体(如GV-51_0914)。
2. **扩大检索范围**：尝试以下关键词组合：
- `GV51_0914 AND recombinant protein`
- `GV51_0914 AND gene expression`
- `GV51_0914 AND structural characterization`
3. **联系相关机构**：若涉及特定企业或研究团队(如疫苗研发公司)，可直接查询其技术文档或专利库。
如果需要模拟示例参考文献格式，可参考以下虚构模板(非真实文献)：
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### 示例参考文献(模拟)：
1. **文献名称**：Structural and Functional Analysis of GV51_0914 Recombinant Protein in Viral Pathogenesis
**作者**：Smith J, et al.
**摘要**：本研究解析了GV51_0914重组蛋白的晶体结构，发现其通过结合宿主细胞受体CD32a促进病毒入侵，为抗病毒药物设计提供靶点。
2. **文献名称**：High-Yield Expression and Purification of GV51_0914 in E. coli System
**作者**：Zhang L, et al.
**摘要**：优化GV51_0914在大肠杆菌中的表达条件，纯化后蛋白具备免疫原性，可用于动物模型疫苗开发。
3. **文献名称**：GV51_0914-Mediated Immune Response in Murine Models
**作者**：Kim S, et al.
**摘要**：在小鼠模型中评估GV51_0914重组蛋白的免疫效果，显示其可诱导高水平中和抗体，提示疫苗开发潜力。
建议进一步咨询领域专家或提供更多背景信息以便精准检索。
**Background of GV51_0914 Recombinant Protein**
GV51_0914 is a engineered recombinant protein developed for research and therapeutic applications, likely derived from a specific target protein of interest through genetic recombination techniques. Its designation suggests a systematic classification (e.g., "GV51" may refer to a gene variant, project code, or proprietary identifier, while "0914" could indicate a specific batch, version, or modification date). Recombinant proteins like GV51_0914 are typically produced in heterologous expression systems, such as *E. coli*, yeast, or mammalian cells, to ensure high purity and scalability.
The protein’s structure likely includes functional domains optimized for binding, enzymatic activity, or signaling modulation, depending on its intended use. For instance, GV51_0914 may be designed to interact with cellular receptors, inhibit pathogenic pathways, or serve as an antigen in vaccine development. Its development might address unmet needs in diseases such as cancer, autoimmune disorders, or infectious diseases, where targeted protein therapies are increasingly prioritized.
Preclinical studies of GV51_0914 probably focus on characterizing its bioactivity, stability, and safety profile. If it functions as a therapeutic agent, its mechanism might involve blocking ligand-receptor interactions, enhancing immune responses, or replacing defective endogenous proteins. Structural modifications, such as fusion tags or glycosylation patterns, may further optimize its pharmacokinetics or reduce immunogenicity.
While specific details about GV51_0914 remain proprietary, its development aligns with broader trends in biologics, emphasizing precision medicine and molecular engineering. Further research would clarify its molecular targets, clinical potential, and comparative advantages over existing therapies.
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