HEK293 Cells.
Protein is >90% pure as determined SDS-PAGE.
The HEK293 derived recombinant biotinylated protein contains the Coronavirus 2019 CoV-2 Nucleocapsid, Wuhan-Hu-1 strain, amino acids 1-419 fused to His-Avi tag at C-terminal.
The novel coronavirus, now known as SARS-CoV-2, emerged in Wuhan, China in December 2019, causing a viral pneumonia (COVID-19). The virus was first identified in a seafood market.
SARS-CoV-2 shares genetic similarities with other coronaviruses, including a bat coronavirus (SARS-CoV-2) found in Zhoushan, China. Specifically, the receptor-binding domain (RBD) of SARS-CoV-2 is structurally similar to that of SARS-CoV, allowing it to bind to the human ACE2 receptor, an enzyme involved in blood pressure regulation.
While bats are considered the likely natural reservoir of SARS-CoV-2, an intermediate animal host, potentially present at the Wuhan market, is suspected to have played a role in transmission to humans. Analysis suggests that SARS-CoV-2 may have arisen from recombination events between different coronaviruses, particularly in the spike protein region responsible for host cell binding.
This recombinant protein consists of the nucleocapsid protein (amino acids 1-419) of SARS-CoV-2 (Wuhan-Hu-1 strain), expressed in HEK293 cells. It is biotinylated and features a C-terminal His-Avi tag for purification and detection purposes.
This CoV-2 Nucleocapsid protein is provided in a buffer consisting of 50mM Tris, 0.15M NaCl, and Arginine, at a pH of 7.5.
While the lyophilized CoV-2 Nucleocapsid protein is stable at room temperature for up to 3 weeks, it's recommended to store it desiccated at temperatures below -18°C. Once reconstituted, store at 4°C for 2-7 days. For extended storage, freeze at -18°C after adding a carrier protein like HSA or BSA (0.1%). Avoid repeated freeze-thaw cycles.
The protein purity is greater than 90% as determined by SDS-PAGE analysis.
HEK293 Cells.
Purified by Metal-Afinity chromatographic technique.
The Coronavirus 2019 Nucleocapsid (N) protein, specifically the segment spanning amino acids 1-419, is a crucial structural component of the SARS-CoV-2 virus, which is responsible for the COVID-19 pandemic. This protein plays a significant role in the virus’s life cycle, including RNA binding, replication, and packaging into new virions. The biotinylated recombinant form of this protein is widely used in research and diagnostic applications due to its enhanced detection capabilities.
The N protein of SARS-CoV-2 is composed of 419 amino acids and has a molecular weight of approximately 45.6 kDa . It is a positively charged, hydrophobic protein that is predominantly found in the nucleus of infected cells . The protein’s structure is characterized by a high content of random coils (55.13%), which contribute to its flexibility and functionality .
The N protein is highly conserved among coronaviruses, sharing 91% similarity with the SARS-CoV N protein and 49% similarity with the MERS-CoV N protein . This conservation underscores its essential role in the viral life cycle. The protein is involved in several critical functions, including:
Biotinylation is a process that involves the addition of biotin, a small molecule, to proteins. This modification enhances the protein’s detection and purification capabilities, making it highly valuable for research and diagnostic purposes. The biotinylated recombinant N protein is produced using recombinant DNA technology, where the gene encoding the N protein is inserted into an expression vector and introduced into a host cell, such as E. coli or mammalian cells. The host cells then produce the N protein, which is subsequently purified and biotinylated.
The biotinylated recombinant N protein is used in various applications, including: