Recombinant Human SARS coronavirus Nucleoprotein(N)

Code CSB-YP349523HQE
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Source Yeast
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Code CSB-EP349523HQE-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-MP349523HQE
Size Pls inquire
Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names N
Uniprot No. P59595
Alternative Names N; 9aNucleoprotein; Nucleocapsid protein; NC; Protein N
Species Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome coronavirus)
Expression Region 1-422
Protein Length full length protein
Tag Info The following tags are available.
N-terminal His-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization 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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°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.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

(From Uniprot)
Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. May modulate transforming growth factor-beta signaling by binding host SMAD3.
Gene References into Functions
  1. The severe acute respiratory syndrome coronavirus N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase, thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I) and inhibiting TRIM25-mediated RIG-I ubiquitination and activation. PMID: 28148787
  2. Electrostatic repulsion acts as a switch to regulate SARS virus N protein oligomerization. PMID: 23717688
  3. These results suggest that SARS coronavirus could reduce pyruvate kinase activity via its nucleocapsid protein, and this may in turn cause disease. PMID: 22222284
  4. The co-localization of SARS-CoVN and CXCL16 in the cytoplasm of HEK293FT cells was also shown using confocal laser scanning microscopy. PMID: 20960183
  5. The HLA-A 2402 complexed with SARSV N1 showed a novel host strategy to present an immunodominant CTL epitope by intrachain hydrogen bond as a featured epitope. PMID: 20844028
  6. SARS-CoV N interacts with MAP19 and increased the expression of MAP19 in cells. PMID: 19737459
  7. This is the first report showing the ability of the nucleocapsid protein of SARS-CoV to induce apoptosis and actin reorganization in mammalian cells under stressed conditions. PMID: 15294014
  8. analysis of SARS-CoV nucleocapsid protein expressed in insect cells PMID: 15514849
  9. The nucleocapsid protein of the SARS coronavirus was cloned and purified. PMID: 15523835
  10. Binding to cyclophilin A during invasion of host cells. PMID: 15688292
  11. coronavirus N protein undergoes posttranslational modification by sumoylation; functional implication of this modification in the formation of coronavirus ribouncleoprotein complex, virion assembly and virus-host interactions PMID: 15848177
  12. the nucleocapsid protein forms a dimer through its C-terminal domain PMID: 15849181
  13. Differences in nuclear/nucleolar localization properties of N from other members of coronavirus family suggest a unique shuttle protein function for N, which may play an important role in the pathogenesis of SARS. PMID: 15992957
  14. results showed that the SARS-CoV N protein can significantly activate NF-kappaB only in Vero E6 cells, which are susceptible to SARS-CoV infection, but not in Vero or HeLa cells; suggests that NF-kappaB activation is cell-specific PMID: 16143815
  15. The secondary structure of the dimerization domain consists of five alpha helices and a beta-hairpin. PMID: 16214138
  16. Results show that the N protein consists of two non-interacting structural domains, the N-terminal RNA-binding domain (RBD) (residues 45-181) and the C-terminal dimerization domain (residues 248-365) (DD), surrounded by flexible linkers. PMID: 16228284
  17. data suggest that the SR-rich motif of the SARS-CoV N protein might play an import role in the transformation of the SARS-CoV N protein between the dimer and multimer during its binding to its central region for self-association or dissociation PMID: 16285739
  18. cytoplasmic localization was directed by region III and was the dominant localization signal in the N protein. PMID: 16298975
  19. the S phase inhibitory activity of the N protein may have major significance during viral pathogenesis PMID: 16431923
  20. the N protein has a dimer with extensive interactions between the two subunits, suggesting that the dimeric form of the N protein is the functional unit in vivo PMID: 16627473
  21. using the solution structure of severe acute respiratory (SARS) coronavirus N-protein, revealed that this motif is available for interaction with cellular factors which may mediate nucleolar localization PMID: 16734668
  22. This is the first report demonstrating the interaction of hUbc9 with a structural protein of plus-strand RNA viruses, indicating a new drug target for SARS-CoV. PMID: 16998888
  23. the nucleocapsid protein of severe acute respiratory syndrome coronavirus is sumoylated by interaction with Ubc9 PMID: 17037517
  24. characterization of the structures of N protein N-terminal domain in two crystal forms, at 1.17 A (monoclinic) and at 1.85 A (cubic), respectively PMID: 17229691
  25. The C-terminal domain (CTD), spanning residues 248-365 (NP248-365), had stronger nucleic acid-binding activity than the NTD. The crystal structure of the NP248-365 region is solved, suggesting a mechanism for helical RNA packaging in the virus. PMID: 17379242
  26. SARS coronavirus N protein can induce apoptosis of COS-1 cells by activating mitochondrial pathway PMID: 17453707
  27. We also showed that N protein activated IL-6 expression through NF-kappaB by facilitating the translocation of NF-kappaB from cytosol to nucleus. PMID: 17490702
  28. SARS coronavirus nucleocapsid protein interacts with Smad3 and modulates transforming growth factor-beta signaling PMID: 18055455
  29. The experiments revealed that N induces the intrinsic apoptotic pathway, resulting in processing of N at residues 400 and 403 by caspase-6 and/or caspase-3. PMID: 18155731
  30. fgl2 gene transcription induced by the N protein of SARS-CoV was dependent on transcription factor C/EBP alpha binding with its cognate cis-element in fgl2 promoter. PMID: 18390877
  31. It was demonstrated that the N protein of SARS-CoV induces aggregation of EF1, inhibiting protein translation and cytokinesis by blocking F-actin bundling. PMID: 18448518
  32. This study employed the SAIL method to determine the high-quality solution structure of the severe acute respiratory syndrome coronavirus nucleocapsid protein C-terminal domain by NMR. PMID: 18561946
  33. the domain conferring the ability to direct virus-like particle assembly and release in SARS-CoV N is largely contained between residues 168 and 421 PMID: 18592403
  34. Phosphorylation of the arginine/serine motif of the nucleocapsid protein did not significantly affect RNA binding of the nucleocapsid protein but impaired its multimerization ability. PMID: 18631359
  35. This paper describes the work to identify two proteins/protein fragments of N protein and to determine their source. PMID: 18926799
  36. An excessive host immune response against the nucleocapsid protein of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is involved in severe pneumonia caused by SARS-CoV infection. PMID: 18941225
  37. The SARS-CoV N protein is a modular protein containing multiple RNA-binding sites. PMID: 19052082
  38. thermostability of the N-terminal RNA-binding domain (RBD) of the N protein; results showed the thermal-induced unfolding-folding transition of the RBD follows a two-state model with a reversibility >90% PMID: 19254548
  39. SR-rich motif is critical for effective virus replication. PMID: 19370068
  40. SARS-CoV N protein specifically modulates transcription of the FGL2 gene to cause fibrosis and vascular thrombosis. PMID: 19423547

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Subcellular Location Virion. Host endoplasmic reticulum-Golgi intermediate compartment. Host Golgi apparatus. Host cytoplasm, host perinuclear region.
Protein Families Betacoronavirus nucleocapsid protein family
Database Links

KEGG: vg:1489678


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