Rabbit Polyclonal NCAP antibody. Suitable for ELISA, WB, ICC/IF and reacts with Influenza A samples. Cited in 13 publications.
Constituents: Whole serum
| ELISA | WB | ICC/IF | |
|---|---|---|---|
| Influenza A | Expected | Expected | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Influenza A | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Influenza A | Dilution info - | Notes Dilute 1:200 - 1:2000 |
| Species | Dilution info | Notes |
|---|---|---|
Species Influenza A | Dilution info Use at an assay dependent concentration. | Notes - |
Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.
Nucleoprotein, Nucleocapsid protein, Protein N, NP
Rabbit Polyclonal NCAP antibody. Suitable for ELISA, WB, ICC/IF and reacts with Influenza A samples. Cited in 13 publications.
Constituents: Whole serum
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The H1N1 Influenza A virus nucleocapsid protein also known as the nucleoprotein (NP) plays a central role in the encapsidation of the viral RNA genome. With a molecular mass of approximately 56 kDa NP forms ribonucleoprotein (RNP) complexes that are essential in the virus's replication and transcription processes. The NP is expressed in the cytoplasm of infected host cells where it binds to viral RNA facilitating the formation of helical RNP structures. These structures are critical for the stability and function of the viral genome.
The NP participates in the virus life cycle by enabling RNA synthesis and interacting with other viral proteins. As part of the RNP complex it collaborates with the RNA polymerase complex made up of PA PB1 and PB2 proteins. This interaction is essential for the transcription and replication of viral RNA. Additionally NP is known to activate host cell signaling pathways that modulate immune response helping the virus evade immune detection and destruction.
The NP protein interacts mainly with the viral replication and transcription mechanisms. The replication-transcription pathway features the synchronization of NP with the RNA polymerase complex ensuring the efficient synthesis of new viral genome copies. The NP also interacts with signaling pathways that involve host proteins like importins which regulate the nuclear import of the RNP complex important for its function.
NP is intimately associated with influenza outbreaks especially those caused by the H1N1 flu virus. This protein's interaction with host immune pathways can alter the immune response contributing to the virus's pathogenicity. Its relation to influenza is also marked by its role in viral replication where it works alongside the M1 matrix protein to export progeny RNPs from the nucleus. Understanding NP is important in the development of flu antibodies as it presents a valuable target for vaccines and antiviral treatments against H1N1 influenza.
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