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Mouse Anti-Rift Valley Fever Virus (RVFV) Nucleoprotein (NP) Monoclonal Antibody

Cat. No.VD7N207

Product TypeVeterinary Antibodies

Size 100 µg

Product Overview

BioVenic mouse monoclonal antibody is specific for rift valley fever virus nucleoprotein. It can be applied to ELISA, IFA and WB assays of rift valley fever virus nucleoprotein.

Specifications

Application ELISA; IFA; WB
Clonality Monoclonal
Classification Primary Antibody
Clone G1N12
Host Mouse
Target Species Virus
Species Reactivity Virus
Specificity Rift Valley Fever Virus Nucleoprotein
Isotype IgG1
Immunogen Recombinant rift valley fever virus nucleoprotein
Purity > 90%
Conjugation Unconjugated
Buffer 0.02µM Phosphate Buffered Saline, pH 7.4
Physical State Liquid

Target Information

Rift valley fever virus (RVFV) nucleoprotein (N) is a vital component of the virus's ribonucleoprotein complex, which includes the viral RNA genome and other viral proteins. The N protein encapsidates the viral RNA, forming a helical nucleocapsid that is essential for the protection, replication, and transcription of the viral genetic material within the host cell. The N protein is a key player in the virus's life cycle and is considered a potential target for antiviral strategies. Its interaction with the viral RNA is critical for the assembly of new virions, making it an attractive target for the development of therapeutics that could disrupt this process. Inhibiting the N protein's function could impair the virus's ability to replicate, thereby limiting the spread of infection.

Target Rift Valley Fever Virus Nucleoprotein
Taxonomy ID 11588
UniProt ID D3K5I7

Shipping and Storage

This product is shipped with wet ice packs. Store at -20°C on receipt (up to 24 months). Avoid exposure to light. Avoid repeated freezing and thawing as this may denature the antibody.

Documents

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

References

  1. Ferron, François, et al. "The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes." PLoS Pathogens 7.5 (2011): e1002030.
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