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Species reactivity
Nipah virus
Host species
Human
Isotype
IgG1
Clonality
Monoclonal
Target
Fusion glycoprotein F0, Protein F, Fusion glycoprotein F2, Fusion glycoprotein F1, F
Concentration
3.14 mg/ml
Endotoxin level
Please contact with the lab for this information.
Purity
>95% as determined by SDS-PAGE.
Purification
Protein A/G purified from cell culture supernatant.
Accession
Applications
ELISA, Neutralization
Form
Liquid
Storage buffer
0.01M PBS, pH 7.4.
Stability and Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at 4°C short term (1-2 weeks). Store at -20°C 12 months. Store at -80°C long term.
Clone ID
1A9
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产品组分
内容
型号
规格 储存温度
InVivoMAb抗尼帕病毒(NiV)融合前抗体(1A9)
VVV08103-01 50ug -20°C InVivoMAb抗尼帕病毒(NiV)融合前抗体(1A9)
VVV08103-02 1mg -20°C 操作手册
1 1 常温室温
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文件资源
文件下载
文件内容
资源说明
VVV08103-InVivoMAb抗尼帕病毒(NiV)融合前抗体(1A9)
操作手册 VVV08103-InVivoMAb抗尼帕病毒(NiV)融合前抗体(1A9)相关单页
宣传单页 -
营销中心
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注意事项
保存建议 厂家推荐蓝冰运输。当您收到产品后，按照说明书建议保存于-20°C。 -
FAQ
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Wang, Y., Fan, L., Ye, P., Wang, Z., Liang, C., Liu, Q., Yang, X., Long, Z., Shi, W., Zhou, Y., et al. (2024). A novel transcription and replication-competent virus-like particles system modelling the Nipah virus life cycle. Emerg Microbes Infect 13, 2368217. PMID: 38865205
Novel transcription and replication-competent virus-like particles system modelling the Nipah virus life cycle. [VVV08103]
Potent Cross-neutralizing Antibodies Reveal Vulnerabilities of Henipavirus Fusion Glycoprotein., PMID:40298900
Structural biology of Nipah virus G and F glycoproteins: Insights into therapeutic and vaccine development., PMID:40261700
Structural and antigenic characterization of novel and diverse Henipavirus glycoproteins., PMID:39713338
How a paramyxovirus fusion/entry complex adapts to escape a neutralizing antibody., PMID:39396053
Immunogenicity and Neutralization of Recombinant Vaccine Candidates Expressing F and G Glycoproteins against Nipah Virus., PMID:39340029
Universal paramyxovirus vaccine design by stabilizing regions involved in structural transformation of the fusion protein., PMID:38821950
Structure and design of Langya virus glycoprotein antigens., PMID:38593070
Therapeutic administration of a cross-reactive mAb targeting the fusion glycoprotein of Nipah virus protects nonhuman primates., PMID:38569014
Prefusion stabilization of the Hendra and Langya virus F proteins., PMID:38214525
Structure and antigenicity of divergent Henipavirus fusion glycoproteins., PMID:37328468
Structural basis for antibody recognition of vulnerable epitopes on Nipah virus F protein., PMID:36932063
A platform technology for generating subunit vaccines against diverse viral pathogens., PMID:36059532
Chimeric Fusion (F) and Attachment (G) Glycoprotein Antigen Delivery by mRNA as a Candidate Nipah Vaccine., PMID:34956199
Broadly neutralizing antibody cocktails targeting Nipah virus and Hendra virus fusion glycoproteins., PMID:33927387
Structure-Based Design of Nipah Virus Vaccines: A Generalizable Approach to Paramyxovirus Immunogen Development., PMID:32595632
A structural basis for antibody-mediated neutralization of Nipah virus reveals a site of vulnerability at the fusion glycoprotein apex., PMID:31767754
An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections., PMID:31570878
Biochemical, conformational, and immunogenic analysis of soluble trimeric forms of henipavirus fusion glycoproteins., PMID:22915804
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