Viral Antigens
Product List
SARS Nucleocaspid (2-422), HEK
SARS Nucleocaspid (2-422 a.a.), HEK Recombinant
The HEK293 derived recombinant protein contains the SARS Coronavirus Nucleoprotein, amino acids 2-422 fused to a 6 His tag at N-terminal.
SARS Spike (14-1195)
SARS Associated Coronavirus Spike (14-1195 a.a.) Recombinant
SARS Spike produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1188 amino acids (14-1195 aa) and having a molecular mass of 131.9kDa.
SARS Spike is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
SARS Spike (14-667)
SARS Spike (14-667 a.a.), Recombinant
The HEK293 derived recombinant protein contains the SARS Coronavirus Spike S1 Gycoprotein, amino acids 14-667 fused to His tag at C-terminal.
SARS Spike (1-53, 90-115, 171-205)
SARS-Associated Coronavirus Spike (1-53, 90-115, 171-205 a.a.), Recombinant
The E.coli derived recombinant protein contains the Spike (1-53, 90-115, 171-205 a.a.) protein immunodominant regions fused to 6xHis tag at C-terminal.
SARS Spike (1-666)
SARS Spike (1-666 a.a.), Recombinant
The HEK293 derived recombinant protein contains the SARS Coronavirus Spike S1 Gycoprotein, amino acids 1-666 fused to His tag at C-terminal.
SARS Spike (306-515)
Coronavirus Spike Receptor Binding Domain (306-515 a.a.), Recombinant
The recombinant SARS Spike containing a total of 220 amino acids (306-515) and having a calculated Mw of 24.8 kDa.
SARS Spike is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
SARS Spike (306-515), Sf9
Coronavirus Spike Receptor Binding Domain (306-515 a.a.)Recombinant, Sf9
SARS Spike produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 219 amino acids (306-515 aa) and having a molecular mass of 24.7kDa.
SARS Spike is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
SARS Spike (306-527)
SARS Spike Receptor Binding Domain(306-527 a.a.), Recombinant
The HEK293 derived recombinant protein contains the SARS Coronavirus spike S glycoprotein Receptor Binding Domain, amino acids 306-527 fused to His tag at C-terminal.
SARS Spike (408-470, 540-573)
SARS-Associated Coronavirus Spike (408-470, 540-573 a.a.), Recombinant
The E.coli derived recombinant protein contains the Spike (408-470, 540-573 a.a.) protein immunodominant regions fused to 6xHis tag at C-terminal.
SARS Spike Mosaic
SARS-Associated Coronavirus Spike Mosaic, Recombinant
The E.coli derived recombinant protein contains the Spike Mosaic protein immunodominant regions 20-210 a.a. fused to 6xHis tag at C-terminal.
Introduction
Severe Acute Respiratory Syndrome (SARS) is a viral respiratory illness caused by a coronavirus known as SARS-CoV. It was first identified in 2003 during an outbreak that began in China and spread to other countries . SARS-CoV belongs to the family Coronaviridae, which is divided into four genera: Alpha, Beta, Gamma, and Delta coronaviruses . SARS-CoV is classified under the Betacoronavirus genus.
Key Biological Properties: SARS-CoV is an enveloped, positive-sense, single-stranded RNA virus. It has a crown-like appearance due to spike proteins on its surface .
Expression Patterns and Tissue Distribution: SARS-CoV primarily infects the respiratory tract, but it can also affect other organs such as the gastrointestinal tract, liver, and kidneys . The virus binds to the angiotensin-converting enzyme 2 (ACE2) receptor, which is widely distributed in various tissues, including the lungs, heart, and intestines .
Primary Biological Functions: The primary function of SARS-CoV is to replicate within host cells. The virus hijacks the host’s cellular machinery to produce viral RNA and proteins, leading to the assembly of new virions .
Role in Immune Responses and Pathogen Recognition: SARS-CoV triggers an immune response by activating various immune cells and signaling pathways. The spike protein of the virus is recognized by the host’s immune system, leading to the production of neutralizing antibodies .
Mechanisms with Other Molecules and Cells: SARS-CoV enters host cells by binding to the ACE2 receptor and undergoing proteolytic cleavage by host cell proteases such as TMPRSS2 . This facilitates viral entry and fusion with the host cell membrane.
Binding Partners and Downstream Signaling Cascades: The binding of SARS-CoV to ACE2 triggers downstream signaling cascades that modulate immune responses and inflammation. The virus can also evade immune detection by interfering with interferon signaling pathways .
Transcriptional Regulation: The expression of SARS-CoV genes is tightly regulated by viral and host factors. Transcription factors such as SP1 and HNF4α play crucial roles in regulating the expression of the ACE2 receptor, which is essential for viral entry .
Post-Translational Modifications: SARS-CoV proteins undergo various post-translational modifications, including phosphorylation, glycosylation, and ubiquitination, which are critical for viral replication and immune evasion .
Biomedical Research: SARS-CoV has been extensively studied to understand viral pathogenesis and host immune responses. This research has led to the development of diagnostic tools and therapeutic strategies .
Diagnostic Tools: Techniques such as polymerase chain reaction (PCR) and enzyme-linked immunosorbent assay (ELISA) are used to detect SARS-CoV infection .
Therapeutic Strategies: Antiviral drugs, monoclonal antibodies, and vaccines have been developed to combat SARS-CoV infection. These therapeutic strategies target various stages of the viral life cycle .
Throughout the Life Cycle: SARS-CoV plays a critical role in the viral life cycle, from initial infection to replication and assembly of new virions. The virus hijacks the host’s cellular machinery to produce viral RNA and proteins, leading to the assembly of new virions . The N protein of SARS-CoV is essential for packaging the viral RNA into new virions and facilitating their release from host cells .
