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Description
H1N1 NP (A/Puerto Rico/8/1934) His Tag, InfluenzaProduct Specification Species Influenza Antigen NP Nucleoprotein Synonyms Nucleoprotein, Nucleocapsid protein, NP. Accession Accession#: P03466 Amino Acid Sequence Met1 Asn498, with C terminal 10*His
Product Specification
| Species | Influenza |
| Antigen | NP/Nucleoprotein |
| Synonyms | Nucleoprotein, Nucleocapsid protein, NP. |
| Accession | Accession#: P03466 |
| Amino Acid Sequence | Met1-Asn498, with C-terminal 10*His MASQGTKRSYEQMETDGERQNATEIRASVGKMIGGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVNGKWMRELILYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELVRMIKRGINDRNFWRGENGRKTRIAYERMCNILKGKFQTAAQKAMMDQVRESRNPGNAEFEDLTFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEREGYSLVGIDPFRLLQNSQVYSLIRPNENPAHKSQLVWMACHSAAFEDLRVLSFIKGTKVLPRGKLSTRGVQIASNENMETMESSTLELRSRYWAIRTRSGGNTNQQRASAGQISIQPTFSVQRNLPFDRTTIMAAFNGNTEGRTSDMRTEIIRMMESARPEDVSFQGRGVFELSDEKAASPIVPSFDMSNEGSYFFGDNAEEYDNGGGSGGGSHHHHHHHHHH. |
| Expression System | Hi5(Baculovirus-InsectCells) |
| Molecular Weight | 57-60 kDa |
| Purity | ＞95% by SDS-PAGE and HPLC |
| Endotoxin | <0.1EU/μg |
| Conjugation | Unconjugated |
| Tag | His Tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | 1*PBS, 1mM DTT, 1mM EDTA, pH7.4 |
| Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
| Stability & Storage | 12 months from date of receipt, -20 to -70 °C as supplied; 6 months, -20 to -70 °C under sterile conditions after reconstitution; 1 week, 2 to 8 °C under sterile conditions after reconstitution; Please avoid repeated freeze-thaw cycles. |
| Reference | 1.Pang B, Cheung NN, Zhang W, Dai J, Kao RY, Zhang H, Hao Q. Structural Characterization of H1N1 Nucleoprotein-Nucleozin Binding Sites. Sci Rep. 2016 Jul 11;6:29684. doi: 10.1038/srep29684. PMID: 27404920; PMCID: PMC4939526.2.Ortega J, Martín-Benito J, Zürcher T, Valpuesta JM, Carrascosa JL, Ortín J. Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification. J Virol. 2000 Jan;74(1):156-63. doi: 10.1128/jvi.74.1.156-163.2000. PMID: 10590102; PMCID: PMC111524. |
Background
Nucleoprotein, encoded by influenza A virus, is an attractive target due to its high conservative and multifunctional nature during virus life cycle. In addition, NP does not have any counterpart in the cell, and hence compounds targeting NP might have less off-target side effects. NP encapsulates the negative strand viral RNA by is binding to 24 bases of RNA, protecting it from nucleases. The encapsulated genomic RNA is termed the ribonucleoprotein (RNP). The active RNP imports into the nucleus through cellular importin α/β pathways, and serves as template for transcription and replication.
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