Recombinant Lassa Virus Nucleoprotein (N) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10629P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed strain Mouse/Sierra Leone/Josiah/1976)(LASV) N.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed strain Mouse/Sierra Leone/Josiah/1976)(LASV) N.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed strain Mouse/Sierra Leone/Josiah/1976)(LASV) N.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed strain Mouse/Sierra Leone/Josiah/1976)(LASV) N.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed strain Mouse/Sierra Leone/Josiah/1976)(LASV) N.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed strain Mouse/Sierra Leone/Josiah/1976)(LASV) N.

Recombinant Lassa Virus Nucleoprotein (N) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10629P
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Product Overview

Description Recombinant Lassa Virus Nucleoprotein (N) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P13699
Target Symbol N
Synonyms N; Nucleoprotein; EC 3.1.13.-; Nucleocapsid protein; Protein N
Species strain Mouse/Sierra Leone/Josiah/1976)(LASV)
Expression System Yeast
Tag N-6His
Target Protein Sequence MSASKEIKSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSEVSNVQRLMRKERRDDNDLKRLRDLNQAVNNLVELKSTQQKSILRVGTLTSDDLLILAADLEKLKSKVIRTERPLSAGVYMGNLSSQQLDQRRALLNMIGMSGGNQGARAGRDGVVRVWDVKNAELLNNQFGTMPSLTLACLTKQGQVDLNDAVQALTDLGLIYTAKYPNTSDLDRLTQSHPILNMIDTKKSSLNISGYNFSLGAAVKAGACMLDGGNMLETIKVSPQTMDGILKSILKVKKALGMFISDTPGERNPYENILYKICLSGDGWPYIASRTSITGRAWENTVVDLESDGKPQKADSNNSSKSLQSAGFTAGLTYSQLMTLKDAMLQLDPNAKTWMDIEGRPEDPVEIALYQPSSGCYIHFFREPTDLKQFKQDAKYSHGIDVTDLFATQPGLTSAVIDALPRNMVITCQGSDDIRKLLESQGRKDIKLIDIALSKTDSRKYENAVWDQYKDLCHMHTGVVVEKKKRGGKEEITPHCALMDCIMFDAAVSGGLNTSVLRAVLPRDMVFRTSTPRVVL
Expression Range 1-569aa
Protein Length Full Length
Mol. Weight 65.0kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. The increased presence of protein N in host cell does not seem to trigger the switch from transcription to replication as observed in other negative strain RNA viruses. Through the interaction with host IKBKE, strongly inhibits the phosphorylation and nuclear translocation of host IRF3, a protein involved in interferon activation pathway, leading to the inhibition of interferon-beta and IRF3-dependent promoters activation. Encodes also a functional 3'-5' exoribonuclease that degrades preferentially dsRNA substrates and thereby participates in the suppression of interferon induction.
Subcellular Location Virion. Host cytoplasm.
Protein Families Arenaviridae nucleocapsid protein family
Database References

Gene Functions References

  1. Importantly, authors demonstrate for the first time that Lassa virus nucleoprotein is involved in the inhibition of antigen-presenting cell-mediated NK cell responses. PMID: 25253342
  2. These results highlight the key role of nucleoprotein exonuclease domain function in the immune evasion that occurs during Lassa virus infection. PMID: 25253344
  3. NP trimerization is essential for transcription and/or replication of the viral genome. PMID: 23553456
  4. molecular dynamics (MD) simulations have been carried out to investigate the characters of deoxythymidine triphosphate binding to two forms of nucleoprotein. PMID: 22871039
  5. Structure of the Lassa virus nucleoprotein revealed by X-ray crystallography, small-angle X-ray scattering, and electron microscopy PMID: 21917929
  6. Residues D389 and G392 of nucleoprotein were critical for Lassa virus viability, while the D389A/G392A and D389T/392A double mutants were severely altered in the ability to suppress interferon in macrophages and dendritic cells. PMID: 21880754

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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