Recombinant Influenza A virus Nucleoprotein(NP)

Code CSB-YP356056IFZ
Size US$1916
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names NP
Uniprot No. P03466
Research Area Others
Alternative Names NP; Nucleoprotein; Nucleocapsid protein; Protein N
Species Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Source Yeast
Expression Region 1-498aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 58.2kDa
Protein Length Full Length
Tag Info N-terminal 6xHis-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function 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.
Gene References into Functions
  1. Taking these observations together, TRIM41 is a constitutively expressed intrinsic influenza A virus restriction factor that targets viral NP for ubiquitination and protein degradation. PMID: 29899090
  2. Structure of importin-alpha bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein has been reported. PMID: 26456934
  3. Immunoprecipitation studies revealed influenza A virus NS1 and NP as direct interaction partners of DDX3. PMID: 26792746
  4. Residue 88 of NP interacts with polymerase PB2 and contributes to influenza A virus replication. PMID: 25043584
  5. HMGB1 protein binds to influenza virus nucleoprotein and promotes viral replication. PMID: 22696656
  6. These results indicate that the PB2, PA, NP, and M segments play a more important role than the remaining four viral RNAs during the genome-packaging process. PMID: 22532680
  7. Data suggest that the flexibility of loops 1 and 2 is required for RNA sampling and binding which likely involve conformational change(s) of the nucleoprotein. PMID: 22272272
  8. These findings demonstrate that replication of the virus genome is followed by its encapsidation by NP in collaboration with its chaperone UAP56. PMID: 21507964
  9. Because the authors showed that NP lacking RNA-binding activity binds directly to the viral polymerase, it is likely that a direct interaction between NP and the viral polymerase results in a modification of the polymerase in favor of unprimed initiation. PMID: 18945782
  10. The authors identified a late-acting defect in NP that, separate from its function in RNA synthesis, indicates a role for the polypeptide in virion assembly, most likely involving M1 as a partner. PMID: 18987140
  11. respective conserved amino acids in NP may thus be critical for the assembly and/or incorporation of sets of eight viral-RNA segments PMID: 19225007

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Subcellular Location Virion, Host nucleus
Protein Families Influenza viruses nucleoprotein family
Database Links

KEGG: vg:956531

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