- ￥1868
- abinScience
- France
- VK031012
- 2025年08月13日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.
- 保质期：
1 year
- 英文名：
Recombinant FHV-1 glycoprotein E/gE Protein, N-His
- 库存：
999
- 供应商：
abinScience
- 规格：
100ug
| Product name | Recombinant FHV-1 glycoprotein E/gE Protein, N-His |
|---|---|
| Catalog No. | VK031012 |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| Purity | >90% as determined by SDS-PAGE. |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Endotoxin level | Please contact with the lab for this information. |
| Expression system | E. coli |
| Accession | YP_003331591.1 |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Alternative Names | envelope glycoprotein E, US8 |
| Species | Felid alphaherpesvirus 1 |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
abinScience, founded in 2023 in Strasbourg, France, is committed to developing and producing high-quality life science reagents. Rooted in one of Europe’s leading hubs for scientific innovation, abinScience empowers global research through reliable, efficient experimental solutions. Guided by the vision of “Empowering Bioscience Discovery,” we support scientists worldwide in advancing the frontiers of bioscience.
Technology and Innovation
Relying on the global leading position in antibody and protein research and more than 20 years of industry experience of its parent company ProteoGenix since 2003...
Product categories and application fields.
Main products...
Application field: Infectious disease research, Neuroscience, Immunology, Oncology
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文献和实验• Rational optimization of glycoprotein E (gE)-encoding mRNA for improved Varicella-zoster virus mRNA vaccine development., PMID:39137287
• Immune Responses to a Recombinant Glycoprotein E Herpes Zoster Vaccine in Adults Aged 50 Years or Older., PMID:29529222
• Varicella zoster virus glycoprotein E facilitates PINK1/Parkin-mediated mitophagy to evade STING and MAVS-mediated antiviral innate immunity., PMID:38184594
• The Adjuvanted Recombinant Zoster Vaccine Confers Long-Term Protection Against Herpes Zoster: Interim Results of an Extension Study of the Pivotal Phase 3 Clinical Trials ZOE-50 and ZOE-70., PMID:34283213
• The immunogenicity and the safety of the adjuvanted glycoprotein E (gE)-based recombinant vaccine against herpes zoster (RZV) in cancer patients during immunotherapy., PMID:38037900
• Alphaherpesvirus glycoprotein E: A review of its interactions with other proteins of the virus and its application in vaccinology., PMID:35992696
• Glycoprotein E-Displaying Nanoparticles Induce Robust Neutralizing Antibodies and T-Cell Response against Varicella Zoster Virus., PMID:39337359
• Immunogenicity and safety of the adjuvanted recombinant zoster vaccine in patients with solid tumors, vaccinated before or during chemotherapy: A randomized trial., PMID:30707761
• Immunogenicity and Safety of the Adjuvanted Recombinant Zoster Vaccine in Chronically Immunosuppressed Adults Following Renal Transplant: A Phase 3, Randomized Clinical Trial., PMID:30843046
Monitoring Recombinant Glycoprotein Heterogeneity
recombinant protein in vivo (1 ). Glycosylation is the most extensive source of protein heterogeneity, and many recent developments in analytical biotechnology have enhanced the ability to monitor and structurally define changes in oligosaccharides associated
N-Linked Protein Glycosylation in a Bacterial System
and permethylation followed by mass spectrometry. We also describe the expression and immunodetection of the model N -glycoprotein, AcrA, fused to a hexa-histidine tag to follow protein glycosylation in C. jejuni . This chapter concludes with the recent demonstration
Analysis of Laminin Structure and Function with Recombinant Glycoprotein Expressed in Insect Cells
Recent developments in the application of eukaryotic recombinant protein techniques have provided new tools with which to dissect and map functional activities in basement membrane glycoproteins. This has been particularly valuable
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