Nucleoprotein/NP Protein, Influenza A virus H1N1 (His-SUMO)

Nucleoprotein/NP Protein, a key component of the influenza virus, plays a vital role in viral replication and transcription. It binds to viral RNA, forming a ribonucleoprotein complex essential for viral genome replication. NP Protein also interacts with host proteins, contributing to viral pathogenesis and immune evasion. Understanding the functions of NP Protein can aid in the development of antiviral strategies against influenza infections. Nucleoprotein/NP Protein, Influenza A virus H1N1 (His-SUMO) is the recombinant Virus-derived Nucleoprotein/NP protein, expressed by E. coli , with N-SUMO, N-6*His labeled tag. The total length of Nucleoprotein/NP Protein, Influenza A virus H1N1 (His-SUMO) is 498 a.a., with molecular weight of ~72.1 kDa.

The nucleoprotein (NP) protein plays a crucial role in viral replication by encapsidating the negative strand viral RNA, providing protection against nucleases. This encapsidated genomic RNA forms the ribonucleoprotein (RNP), which serves as a template for transcription and replication. To initiate the infectious cycle, the RNP needs to be localized in the host nucleus, but its large size prevents diffusion through the nuclear pore complex. NP contains two nuclear localization signals that actively facilitate RNP import into the nucleus via the cellular importin alpha/beta pathway. During later stages of infection, nuclear export of RNPs is mediated by viral proteins NEP, which interacts with M1, binding to nucleoproteins. There is a possibility that nucleoprotein directly binds to host exportin-1/XPO1 and actively participates in RNPs nuclear export. M1's interaction with RNP appears to conceal nucleoprotein's nuclear localization signals. However, upon infecting a new cell, M1 dissociates from the RNP due to acidification of the virion driven by M2 protein. This dissociation unveils nucleoprotein's nuclear localization signals, leading to targeted RNP transport into the nucleus. Additionally, nucleoprotein forms homomultimers to create the nucleocapsid and may bind to host exportin-1/XPO1. Protein-RNA interactions involve a combination of electrostatic interactions between positively charged residues and the phosphate backbone, as well as planar interactions between aromatic side chains and bases.

Virus

E. coli

N-SUMO;N-6*His

P18071 (M1-N498)

/

MASQGTKRSYEQMETDGDRQNATEIRASVGKMIDGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYKRVDGKWMRELVLYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDTTYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELIRMIKRGINDRNFWRGENGRKTRIAYERMCNILKGKFQTAAQRAMMDQVRESRNPGNAEIEDLIFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEKEGYSLVGIDPFKLLQNSQVYSLIRPNENPAHKSQLVWMACNSAAFEDLRVSSFIRGTKVIPRGKLSTRGVQIASNENMDTMGSSTLELRSRYWAIRTRSGGNTNQQRASAGQISIQPTFSVQRNLPFDKTTIMAAFTGNAEGRTSDMRAEIIRMMESARPEEVSFQGRGVFELSDERAANPIVPSFDMSNEGSYFFGDNAEEYDN

Approximately 72.1kDa

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  Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm sterile filtered PBS, 6% Trehalose, pH 7.4.

<17 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.