| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GP |
| Uniprot No | P55259 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-537aa |
| 氨基酸序列 | MPHLMERMVGSGLLWLALVSCILTQASAVQRGYGNPIEASSYGLDLDCGAPGTPEAHVCFDPCQNYTLLDEPFRSTENSAGSQGCDKNMSGWYRFVGEGGVRMSETCVQVHRCQTDAPMWLNGTHPALGDGITNHTACAHWSGNCCFWKTEVLVKACPGGYHVYRLEGTPWCNLRYCTVPRDPSTVEDKCEKACRPEEECLALNSTWGCFCRQDLNSSDVHSLQPQLDCGPREIKVKVDKCLLGGLGLGEEVIAYLRDPNCSSILQTEERNWVSVTSPVQASACRNILERNQTHAIYKNTLSLVNDFIIRDTILNINFQCAYPLDMKVSLQAALQPIVSSLNVSVDGNGEFIVRMALFQDQNYTNPYEGDAVELSVESVLYVGAILEQGDTSRFNLVLRNCYATPTEDKADLVKYFIIRNSCSNQRDSTIHVEENGQSSESRFSVQMFMFAGHYDLVFLHCEIHLCDSLNEQCQPSCSRSQVRSEVPAIDLARVLDLGPITRRGAQSPGVMNGTPSTAGFLVAWPMVLLTVLLAWLF |
| 预测分子量 | 59,4 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条关于GP重组蛋白的参考文献示例(注：文献信息为虚构，仅供格式参考)：
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1. **文献名称**：*Structural and Functional Characterization of Recombinant Ebola Virus Glycoprotein*
**作者**：Smith, J. et al.
**摘要**：本研究通过哺乳动物表达系统成功表达并纯化埃博拉病毒GP重组蛋白，解析其三维结构，并验证其在假病毒模型中诱导中和抗体的能力，为疫苗开发提供依据。
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2. **文献名称**：*Expression Optimization of SARS-CoV-2 Spike Glycoprotein in Insect Cells*
**作者**：Zhang, L. & Wang, H.
**摘要**：利用杆状病毒-昆虫细胞系统优化新冠病毒刺突糖蛋白(S蛋白)的重组表达，实现高产量和正确糖基化修饰，为诊断试剂和亚单位疫苗生产奠定基础。
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3. **文献名称**：*GP1 Recombinant Protein as a Therapeutic Target for Lassa Fever*
**作者**：Johnson, R. et al.
**摘要**：通过大肠杆菌表达系统制备拉沙病毒GP1重组蛋白，证明其在小鼠模型中可有效阻断病毒入侵宿主细胞，为抗病毒药物研发提供新策略。
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如需真实文献，建议通过PubMed或Web of Science检索关键词(如"recombinant glycoprotein"或"GP protein expression")获取近年研究。
**Background of GP Recombinant Proteins**
Glycoprotein (GP) recombinant proteins are engineered versions of viral or cellular glycoproteins produced through genetic recombination techniques. These proteins play pivotal roles in biomedical research, therapeutic development, and diagnostic applications. GPs are critical surface proteins in many viruses, such as Ebola, Lassa, and coronaviruses, where they mediate host cell entry by binding to receptors and facilitating membrane fusion. Recombinant GP proteins replicate these functional domains *in vitro*, enabling studies on viral pathogenesis, immune responses, and drug discovery.
The production of GP recombinant proteins typically involves cloning the target gene into expression vectors (e.g., bacterial, mammalian, or insect cell systems). Mammalian or insect systems are often preferred for glycosylation accuracy, as many viral GPs require post-translational modifications for proper folding and antigenicity. For example, Ebola virus GP is expressed as a trimeric structure in mammalian cells to mimic its native conformation, essential for vaccine or antibody development.
Applications include **vaccine design** (e.g., Ebola GP-based vaccines like rVSV-ZEBOV), **therapeutic antibodies** (e.g., monoclonal antibodies targeting SARS-CoV-2 Spike GP), and **diagnostic tools** (e.g., ELISA kits using recombinant GP antigens). GP recombinant proteins also aid in structural studies, elucidating mechanisms of viral entry and immune evasion.
Challenges include maintaining protein stability, avoiding misfolding, and balancing glycosylation patterns to ensure immunogenicity without excessive heterogeneity. Advances in protein engineering, such as structure-guided mutagenesis or glycoengineering, continue to refine these proteins for enhanced efficacy and safety.
Overall, GP recombinant proteins are indispensable tools for understanding viral biology and developing countermeasures against emerging infectious diseases, underscoring their importance in global health preparedness.
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