Recombinant Severe acute respiratory syndrome coronavirus 2 Nucleoprotein (N) (Active) CSB-EP3325GMY CUSABIO
$228.00
In stock
SKU
CSB-EP3325GMY
Product Details
| Uniprot No. | P0DTC9 |
| Alternative Names | N; Nucleoprotein; N; Nucleocapsid protein; NC; Protein N |
| Species | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
| Source | E.coli |
| Expression Region | 1-419aa |
| Purity | Greater than 85% as determined by SDS-PAGE. |
| Endotoxin | Less than 1.0 EU/ug as determined by LAL method. |
| Activity | ①Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2-N at 2 μg/ml can bind SARS-CoV-2-N Antibody (CSB-RA33255A1GMY), the EC 50 of SARS-CoV-2-N protein is 1.368 -1.804 ng/ml.②Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2-N at 2 μg/ml can bind SARS-CoV-2-N Antibody (CSB-RA33255A0GMY), the EC 50 of SARS-CoV-2-N protein is 4.267-5.568 ng/ml. |
| Tag Info | N-terminal 6xHis-tagged |
| Form | Lyophilized powder Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand. |
| Buffer | Lyophilized from a 0.2 μm sterile filtered 20 mM Tris-HCl, 0.5 M NaCl, 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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference. |
| Troubleshooting and FAQs | Protein FAQs |
| Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
| Lead Time | 3-7 business days |
| Target Names | N |
| Research Area | Microbiology |
| Target Protein Sequence | MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRNSSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYTAAIKLDDKDPNFKDQVILLNKHIDAYKTFPPTEPKKDKKKKADETQALPQRQKKQQTVTLLPAADLDDFSKQLQQSMSSADSTQA |
| Mol. Weight | 49.7 kDa |
| Protein Length | Full Length |
| 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. |
| Datasheet & COA | Please contact us to get it. |
| Description | Recombinant severe acute respiratory syndrome coronavirus 2 Nucleoprotein (N) production starts with the isolation of the target gene, incorporating an N-terminal 6xHis-tag to aid in purification. This target gene encoding the1-419aa of the SARS-CoV-2 N protein is inserted into an expression vector, which is subsequently introduced into an E. coli using transformation techniques. The E. coli cell expresses the protein, which accumulates within the cells. The protein is subsequently collected typically through cell lysis and purified using affinity chromatography. Finally, the protein’s activity and functionality are confirmed through functional ELISA tests. It has been demonstrated to be an active protein. Its endotoxin content is less than 1.0 EU/ug as determined by the LAL method. Its purity is over 85% as determined by SDS-PAGE. The SARS-CoV-2 Nucleoprotein (N) is a crucial structural protein of the virus that plays various essential roles in the viral life cycle. It is involved in functions such as replication, packaging, and transcription [1]. The N protein is an RNA-binding protein that forms a helical ribonucleoprotein necessary for SARS-CoV-2's RNA transcription and replication [2]. It is highly conserved and abundantly expressed in SARS-CoV-2, making it a prominent target for diagnostic assays [3]. Studies have shown that the N protein can be detected through seropositivity assays, making it a valuable tool for identifying SARS-CoV-2 infections, including breakthrough infections post-vaccination [4]. Furthermore, the N protein has been utilized in the development of biosensors and immunoassays for antigen detection, highlighting its significance in diagnostic technologies [5][6]. The N protein of SARS-CoV-2 has been the subject of proteomic analysis to understand its interactions with host proteins during infection [7]. It has been identified as a potential target for antiviral therapies, with studies exploring the use of compounds like naproxen that target the N protein to inhibit viral replication [8]. The N protein has also been considered a component of vaccine development due to its immunogenic properties [9]. References: [1] I. Mahdi, H. Yeasmin, I. Hossain, R. Badhan, A. Ali, M. Kaiumet al., Potential antiviral peptides against the nucleoprotein of sars-cov-2, Chemical Papers, vol. 77, no. 2, p. 813-823, 2022. https://doi.org/10.1007/s11696-022-02514-4 [2] H. Kim, J. Lee, M. Kim, S. Park, M. Choi, W. Leeet al., Development of a sars-cov-2-specific biosensor for antigen detection using scfv-fc fusion proteins, Biosensors and Bioelectronics, vol. 175, p. 112868, 2021. https://doi.org/10.1016/j.bios.2020.112868 [3] M. Chabi, B. Vu, K. Brosamer, M. Smith, D. Chavan, J. Conradet al., Smartphone-read phage lateral flow assay for point-of-care detection of sars-cov-2 infection,, 2022. https://doi.org/10.26434/chemrxiv-2022-ksshx [4] L. Hoogen, G. Smits, C. Hagen, D. Wong, E. Vos, M. Bovenet al., Seropositivity to nucleoprotein to detect sars-cov-2 infections: a tool to detect breakthrough infections after covid-19 vaccination,, 2021. https://doi.org/10.1101/2021.10.05.21264555 [5] L. Kollhoff, M. Kipping, M. Rauh, U. Ceglarek, G. Barka, F. Barkaet al., Development of a rapid and specific maldi-tof mass spectrometric assay for sars-cov-2 detection,, 2023. https://doi.org/10.1101/2023.03.10.23287091 [6] J. Bong, T. Kim, J. Jung, S. Lee, J. Sung, C. Leeet al., Competitive immunoassay of sars-cov-2 using pig sera-derived anti-sars-cov-2 antibodies, Biochip Journal, vol. 15, no. 1, p. 100-108, 2021. https://doi.org/10.1007/s13206-021-00011-6 [7] F. Ciccosanti, M. Rienzo, A. Romagnoli, F. Colavita, G. Refolo, C. Castillettiet al., Proteomic analysis identifies the rna helicase ddx3x as a host target against sars-cov-2 infection, Antiviral Research, vol. 190, p. 105064, 2021. https://doi.org/10.1016/j.antiviral.2021.105064 [8] B. Terrier, S. Dilly, M. Pizzorno, J. Henri, F. Berenbaum, B. Linaet al., Broad-spectrum antiviral activity of naproxen: from influenza a to sars-cov-2 coronavirus,, 2020. https://doi.org/10.1101/2020.04.30.069922 [9] G. Ahlén, L. Frelin, N. Nikouyan, F. Weber, U. Höglund, O. Larssonet al., The sars-cov-2 n protein is a good component in a vaccine, Journal of Virology, vol. 94, no. 18, 2020. https://doi.org/10.1128/jvi.01279-20 |
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