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AB252771

Anti-Respiratory Syncytial Virus Nucleoprotein antibody [B325M]

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(1 Publication)

Mouse Monoclonal NCAP antibody. Cited in 1 publication. Immunogen corresponding to Virus preparation containing Respiratory Syncytial Virus Nucleoprotein protein.

View Alternative Names

Nucleoprotein, Protein N, Nucleocapsid protein, N

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

B325M

Isotype

IgG1

Carrier free

No

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Specificity

RSV Nucleoprotein (42 kDa).

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Purification notes
>90% pure (SDS-PAGE). Sourced from tissue culture supernatant.
Storage buffer
Preservative: 0.0975% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Respiratory Syncytial Virus Nucleoprotein (RSV N protein) plays a central mechanical role in the replication and transcription of the RSV genome. It binds single-stranded RNA acting as a scaffold for the virus's RNA synthesis. The nucleocapsid protein another name for RSV N protein has a molecular mass of approximately 45 kilodaltons. It is expressed in cells infected by the RSV notably within the cytoplasm forming a protective helix around the viral RNA genome.
Biological function summary

Within the context of viral infection and replication RSV N protein is essential for packaging and protecting the viral RNA genome. It forms part of a complex with the phosphoprotein (P protein) and the large polymerase protein (L protein) to facilitate RNA replication and transcription. This complex ensures the stability and integrity of the viral genome allowing the virus to efficiently replicate and produce infectious particles. Therefore the nucleoprotein strongly influences the life cycle of the virus.

Pathways

The RSV N protein functional capacity is pivotal within the viral RNA transcription and replication pathways. It closely interacts with the phosphoprotein P enhancing the activity of the viral RNA-dependent RNA polymerase complex. This interaction synergistically ties into the virus's replication pathway ensuring the production of viral RNAs. The N protein also coordinates with M2-1 protein in regulating mRNA synthesis and RNA processing reflecting its comprehensive involvement in essential viral pathways.

The involvement of RSV N protein connects strongly to respiratory tract infections particularly in infants and the elderly. RSV infection often leads to bronchiolitis and pneumonia where the N protein plays an important role in propagating the disease. Its interaction with the fusion glycoprotein (F protein) facilitates virus assembly and release which enhances viral spread and subsequent infection severity. Researchers often focus on these proteins when developing therapeutics targeting RSV-related diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases (PubMed : 19965480, PubMed : 23677789, PubMed : 31229488). RNA replication depends on the availability of soluble nucleoprotein (PubMed : 22623798, PubMed : 9299631). The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication (PubMed : 22623798). Together with the phosphoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway (PubMed : 32878896). May also act as a modulator of the innate immune response by sequestration of host IFIH1/MDA5 and MAVS into IBs (PubMed : 22623778).
See full target information N

Publications (1)

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Current protocols 4:e1030 PubMed38923763

2024

Applications of Surface Plasmon Resonance (SPR) to the Study of Diverse Protein-Ligand Interactions.

Applications

Unspecified application

Species

Unspecified reactive species

Dana M Burris,Samuel W Gillespie,Emma Joy Campbell,S Nick Ice,Vikas Yadav,William D Picking,Christian L Lorson,Kamal Singh
View all publications

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