SARS-COV-2 Nucleocapsid Protein CTD Domain Protein 4694

$150.00 – $500.00

Summary

Expression: E.coli
Pure: Yes (SDS-PAGE)
Amino Acid Range: Gly243-Pro364

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SKU: 4694parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	QHD43423.2
express system	E.coli
product tag	N-His-Avi
purity	> 95% as determined by Tris-Bis PAGE
background	Nucleocapsid protein (N) is the major viral structural component; its main function is to protect and encapsidate the viral RNA forming viral RNP complex. It is encoded by the S segment vRNA and is abundantly expressed in the cytoplasm of infected cells.
molecular weight	The protein has a predicted MW of 17 kDa same as Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

SARS-COV-2 Nucleocapsid Protein CTD Domain Protein 4694

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Nucleocapsid protein (N) is the major viral structural component; its main function is to protect and encapsidate the viral RNA forming viral RNP complex. It is encoded by the S segment vRNA and is abundantly expressed in the cytoplasm of infected cells.
Protein names Nucleoprotein (N) (Nucleocapsid protein) (NC) (Protein N)
Gene names N,N
Protein family Betacoronavirus nucleocapsid protein family
Mass 45626Da
Function FUNCTION: 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 (PubMed:33264373). Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Attenuates the stress granules formation by reducing host G3BP1 access to host mRNAs under stress conditions (PubMed:34901782, PubMed:36534661). {ECO:0000269\|PubMed:32974389, ECO:0000269\|PubMed:33264373, ECO:0000269\|PubMed:34901782, ECO:0000269\|PubMed:36534661}.; FUNCTION: May block host chemokine function in vivo, facilitating viral replication and transmission (PubMed:35921414). Acts by being secreted into the extracellular space where it competes to host chemokines for binding to host glycosaminoglycans (GAG) (PubMed:35921414). {ECO:0000269\|PubMed:35921414}.; FUNCTION: May induce inflammasome responses in cultured cells and mice. Acts by interacting with host NLRP3 to facilitate inflammasome assembly, which induces cytokine release that may play a role in COVID lung injury. {ECO:0000269\|PubMed:34341353}.
Subellular location SUBCELLULAR LOCATION: Virion {ECO:0000255\|HAMAP-Rule:MF_04096}. Host cytoplasm {ECO:0000269\|PubMed:33060197, ECO:0000269\|PubMed:34341353}. Secreted {ECO:0000269\|PubMed:35921414}. Host extracellular space {ECO:0000269\|PubMed:35921414}. Note=Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. When located inside the virion, complexed with the viral RNA. Can be secreted by unconventional protein secretion (UPS) (PubMed:35921414). When secreted, can bind to host glycosaminoglycans on infected and non infected cells (PubMed:35921414). Found in host cytoplasmic stress granules (PubMed:34901782). {ECO:0000255\|HAMAP-Rule:MF_04096, ECO:0000269\|PubMed:34901782, ECO:0000269\|PubMed:35921414}.
Structure SUBUNIT: Homodimer, homotetramer, homooligomer with RNA (PubMed:32654247). Both monomeric and oligomeric forms interact with RNA. Interacts with protein M (By similarity). Interacts with protein E (By similarity). Interacts with NSP3; this interaction serves to tether the genome to the newly translated replicase-transcriptase complex at a very early stage of infection (PubMed:35044811). May interact with host NLRP3 (PubMed:34341353). Interacts with host G3BP1; the interaction is enhanced by host HDAC6 which deacetylates the viral N protein and promotes N protein association with G3BP1, disrupting stress granule formation and facilitating viral replication (PubMed:39135075). {ECO:0000250\|UniProtKB:P59595, ECO:0000255\|HAMAP-Rule:MF_04096, ECO:0000269\|PubMed:32654247, ECO:0000269\|PubMed:34341353, ECO:0000269\|PubMed:35044811, ECO:0000269\|PubMed:39135075}.
Post-translational modification PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection. {ECO:0000255\|HAMAP-Rule:MF_04096}.; PTM: Phosphorylated on serine residues by host GSK3A and GSK3B (PubMed:34593624, PubMed:35728038). This promotes the solubility of homodimers that would otherwise aggregate (PubMed:32974389). Host phosphatase would dephosphorylate the protein during assembly at M bound membranes (PubMed:32974389). {ECO:0000269\|PubMed:34593624, ECO:0000269\|PubMed:35728038, ECO:0000305\|PubMed:32974389}.; PTM: Proteolytically cleaved by host CASP6. The cleavage leads to two fragments and facilitates viral replication by inhibiting host IFN signaling. The two fragments may interact with IRF3 inhibiting its nuclear translocation after activation and reduce the expression of IFNB and IFN-stimulated genes. {ECO:0000269\|PubMed:35922005}.; PTM: Acetylated (PubMed:39135075). Deacetylated by host HDAC6 which promotes association of the viral N protein with human G3BP1, disrupting cellular stress granule formation and facilitating viral replication (PubMed:39135075). {ECO:0000269\|PubMed:39135075}.
Target Relevance information above includes information from UniProt accession: P0DTC9
The UniProt Consortium

Data

SDS-PAGE gel of SARS-COV-2 Nucleocapsid Protein CTD Domain Protein

SARS-COV-2 NP CTD Domain on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.