Name:
H1N1 NP Protein
Synonyms:
Nucleoprotein, Nucleocapsid protein, NP.
Species Name:
Influenza
Label Name:
His Tag
Marker Name:
Unconjugated
Accession:
Accession#: P03466
Gene Id:
Met1-Asn498, with C-terminal 10*His MASQGTKRSYEQMETDGERQNATEIRASVGKMIGGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVNGKWMRELILYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELVRMIKRGINDRNFWRGENGRKTRIAYERMCNILKGKFQTAAQKAMMDQVRESRNPGNAEFEDLTFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEREGYSLVGIDPFRLLQNSQVYSLIRPNENPAHKSQLVWMACHSAAFEDLRVLSFIKGTKVLPRGKLSTRGVQIASNENMETMESSTLELRSRYWAIRTRSGGNTNQQRASAGQISIQPTFSVQRNLPFDRTTIMAAFNGNTEGRTSDMRTEIIRMMESARPEDVSFQGRGVFELSDEKAASPIVPSFDMSNEGSYFFGDNAEEYDNGGGSGGGSHHHHHHHHHH.
Molecular Weight:
57-60 kDa
Purity:
＞95% by SDS-PAGE and HPLC
Physical Appearance Name:
Lyophilized Powder
Endotoxin Name:
<0.1EU/μg
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.
Buffer System:
1*PBS, 1mM DTT, 1mM EDTA, pH7.4
Quality Statement:
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.
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.
Related category websites: https://www.medchemexpress.com/recombinant-proteins.html
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