- ￥1668
- abinScience
- China
- VK521063
- 2025年07月25日
- ELISA, SPR, Neutralization
- Human
- Hendra virus, Nipah virus
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- 详细信息
- 文献和实验
- 技术资料
- 免疫原：
Human
- 亚型：
VHH-Fc
- 形态：
Liquid
- 保存条件：
0.01M PBS pH 7.4
- 克隆性：
Monoclonal
- 标记物：
Unconjugated
- 适应物种：
Hendra virus, Nipah virus
- 保质期：
1 year
- 抗原来源：
Human
- 目录编号：
VK521063
- 级别：
科研级别
- 库存：
999
- 供应商：
abinScience
- 宿主：
Human
- 应用范围：
ELISA, SPR, Neutralization
- 浓度：
1mg/mL
- 靶点：
Fusion glycoprotein F0, Protein F, Fusion glycoprotein F2, Fusion glycoprotein F1, F
- 抗体英文名：
Anti-HeV/NiV Fusion Protein Antibody (DS90)
- 抗体名：
Anti-HeV/NiV Fusion Protein Antibody (DS90)
- 规格：
100ul
| Product name | Anti-HeV/NiV Fusion Protein Antibody (DS90) |
|---|---|
| Catalog No. | VK521063 |
| Host species | Human |
| Species reactivity | Hendra virus, Nipah virus |
| Immunogen | / |
| Form | Liquid |
| Storage buffer | 0.01M PBS pH 7.4 |
| Purity | >95% as determined by SDS-PAGE. |
| Clonality | Monoclonal |
| Isotype | VHH-Fc |
| Applications | ELISA, SPR, Neutralization |
| Target | Fusion glycoprotein F0, Protein F, Fusion glycoprotein F2, Fusion glycoprotein F1, F |
| Purification | Protein A/G purified from cell culture supernatant. |
| Endotoxin level | Please contact with the lab for this information. |
| Expression system | / |
| Accession | Q9IH63, O89342 |
| Alternative Names | / |
| Clone ID | DS90 |
| Species | / |
| Product Usage Information | / |
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, abinScience has inherited advanced technologies and high-quality standards. In particular, the XtenCHO™ system developed by ProteoGenix, which has two modes of transient expression and stable expression, has been widely recognized as a core technology to improve the efficiency of protein production, providing a solid foundation for abinScience's product research and development.
Product categories and application fields.
Main products.
10000+ high-activity proteins.
15000+ antibody series products:
Classic monoclonal antibody.
Monoclonal antibody
Internal control antibody, labeled antibody.
High-quality phosphorylation antibodies.
Highly specific nanobodies and small molecule antibodies.
Functional antibodies in vivo.
Low-background flow cytometry antibodies.
DNA/RNA antibodies and PEG antibodies.
1000+ reagent kit series products.
Large-scale packaging customization services: We offer personalized antibody design, protein production, molecular optimization, and experimental development services.
Application field
Infectious disease research: including viruses, superbugs, parasites, etc.
Neuroscience research: Supporting research on neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.
Immunology research: Covers the research needs of immune activation, inhibition, and allergies and abnormal reactions.
Oncology research: Supporting the development of tumor biology and anti-tumor drugs.
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文献和实验• Absence of N-linked glycans from the F2 subunit of the major baculovirus envelope fusion protein F enhances fusogenicity., PMID:17251561
• Activation of the Sendai virus fusion protein (f) involves a conformational change with exposure of a new hydrophobic region., PMID:6259173
• Proteolytic cleavage of the fusion protein but not membrane fusion is required for measles virus-induced immunosuppression in vitro., PMID:10644371
• Antibody against the carboxyl terminus of the F2 subunit of Sendai virus fusion glycoprotein inhibits proteolytic activation., PMID:8389088
• Biosynthesis of mumps virus F glycoprotein: non-fusing strains efficiently cleave the F glycoprotein precursor., PMID:6688088
• Characterization of the infectious salmon anemia virus fusion protein., PMID:16160182
• Intracellular processing, glycosylation, and cell-surface expression of the measles virus fusion protein (F) encoded by a recombinant adenovirus., PMID:2309445
• Effects of N-linked glycosylation of the fusion protein on replication of human metapneumovirus in vitro and in mouse lungs., PMID:21450943
• Nucleotide sequence of the gene encoding the fusion glycoprotein of Newcastle disease virus., PMID:3025345
Expression of Antibody Fusion Proteins in Mammalian Cells
range of recombinant molecules have now been constructed where the binding specificity of an antibody or T-cell receptor variable domain, cytokine, growth factor, or other protein ligand (e.g., CD4) is fused to another protein domain, for example
Expression of Recombinant Antibody Fusion Proteins in E. coli
of the antibody moiety, and local cytotoxic action is determined by the foreign protein. Examples of this approach include immunotoxins, in which the effector protein is a plant or bacterial toxin (1 ), and antibody-directed enzyme prodrug therapy (ADEPT
Antibody-IL2 Fusion Proteins for Tumor Targeting
as part of an antibody-cytokine fusion protein to the tumor tissue by a single chain fragment of variable regions (scFv) antibody recognizing a tumor-associated antigen. IL2 can moreover be combined with IL12 in a dual cytokine fusion protein, which simultaneously
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