SARS-CoV
Description
The Recombinant SARS-CoV Nucleocapsid Protein is manufactured with N-terminal fusion His Tag. The Recombinant SARS-CoV Nucleocapsid His-Tagged Fusion Protein is 47.8kDa containing 437 amino acid residues of the SARS-CoV Nucleocapsid protein and 16 additional amino acid residues – His Tag (underlined).
Product Specs
The Recombinant SARS-CoV Nucleocapsid Protein is engineered with an N-terminal His Tag fusion. This His-Tagged Fusion Protein boasts a molecular weight of 47.8kDa, encompassing 437 amino acid residues of the SARS-CoV Nucleocapsid protein alongside 16 additional amino acid residues constituting the His Tag (underlined).
The product is sterile-filtered (0.4µm) and lyophilized from a 0.5 mg/ml solution in 0.05M Acetate buffer at pH 4.
To create a working stock solution of roughly 0.5mg/ml, reconstitute the lyophilized pellet by adding 0.1M Acetate buffer at pH 4 and allow for complete dissolution. For adjustments to a higher pH, it's recommended to perform an intensive dilution using the appropriate buffer to achieve a concentration of 10µg/ml. The solubility of this antigen is limited at higher concentrations.
For long-term storage, keep the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize freeze-thaw cycles. While the reconstituted protein exhibits stability at 4°C for a limited duration, it demonstrates no discernible changes after two weeks at this temperature.
MRGSHHHHHH GMASHMSDNG PQSNQRSAPR ITFGGPTDST DNNQNGGRNG ARPKQRRPQG LPNNTASWFT ALTQHGKEEL RFPRGQGVPI NTNSGPDDQI GYYRRATRRV RGGDGKMKEL SPRWYFYYLG TGPEASLPYG ANKEGIVWVA TEGALNTPKD HIGTRNPNNN AATVLQLPQG TTLPKGFYAE GSRGGSQASS RSSSRSRGNS RNSTPGSSRG NSPARMASGG GETALALLLL DRLNQLESKV SGKGQQQQGQ TVTKKSAAEA SKKPRQKRTA TKQYNVTQAF GRRGPEQTQG NFGDQDLIRQ GTDYKHWPQI AQFAPSASAF FGMSRIGMEV TPSGTWLTYH GAIKLDDKDP QFKDNVILLN KHIDAYKTFP PTEPKKDKKK KTDEAQPLPQ RQKKQPTVTL LPAADMDDFS RQLQNSMSGA SADSTQA.
Product Science Overview
The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) nucleocapsid (N) protein is a critical structural component of the virus. It plays a pivotal role in the packaging of the viral RNA genome and the formation of the ribonucleoprotein (RNP) complex. The recombinant form of this protein, specifically the 422 amino acid (a.a) variant, has been extensively studied for its structural, functional, and immunogenic properties.
The SARS-CoV nucleocapsid protein is composed of 422 amino acids and is highly conserved among coronaviruses. It is an RNA-binding protein that is essential for the encapsidation of the viral genome. The N protein is divided into two main domains: the N-terminal domain (NTD) and the C-terminal domain (CTD), both of which are involved in RNA binding. Additionally, the protein contains intrinsically disordered regions (IDRs) that contribute to its flexibility and interaction with other viral and host proteins .
The N protein is crucial for the viral life cycle. It facilitates the packaging of the viral RNA into a helical RNP complex, which is then incorporated into new virions. This process is essential for the assembly and release of infectious viral particles. The N protein also plays a role in enhancing the efficiency of viral transcription and replication by interacting with the viral RNA-dependent RNA polymerase .
Due to its high immunogenicity, the N protein is a major target for the host immune response. It elicits strong antibody responses, making it a valuable antigen for serological assays and diagnostic tests. Recombinant forms of the N protein, such as the 422 a.a variant, are used in enzyme-linked immunosorbent assays (ELISAs) to detect antibodies against SARS-CoV in patient samples .
The recombinant SARS-CoV N protein has been extensively used in research to study the virus’s structure, function, and interactions with host proteins. It has also been explored as a potential target for antiviral therapies. By inhibiting the interactions between the N protein and viral RNA or host proteins, it may be possible to disrupt the viral life cycle and reduce viral replication .
