Severe acute respiratory syndrome (SARS) is a lower respiratory tract illness that was first reported in patients from the Guandong Province of China in November 2002.
The causative agent, which was previously unknown, was isolated in 2003 and named as SARS coronavirus (SARS-CoV).
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the coronavirus induced disease 19 (COVID-19) which emerged in China in late 2019, resulting in a worldwide epidemic (Zhou et al., 2020).
Human coronaviruses are the major cause of upper respiratory tract illness.
They are positive-stranded RNA viruses, and contain the largest viral RNA genomes known to date (27-31 kb).
SARS (severe acute respiratory syndrome) and COVID-19 are both caused by human coronaviruses, SARS-CoV and SARS-CoV-2, respectively.
The genome of SARS-CoV-2 shares 82% nucleotide identity with human SARS-CoV and 89% with bat SARS-like-CoVZXC21 (Lu et al., 2020; Zhao et al., 2020).
However, initially it displayed lower pathogenicity and higher human to human transmissibility (Li et al., 2020).
The coronavirus genome encodes four structural proteins: the spike (S) protein, nucleocapsid (N) protein, membrane (M) protein, and the envelope (E) protein.
The S protein assists in the attachment of the virus to the human cell and comprises intracellular, transmembrane, and extracellular regions.
The extracellular region contains the S1 receptor binding subunit (RBD) and the S2 membrane fusion subunit.
Generally, following SARS-CoV-2 infection, antibodies appear after 7–14 days and persist for weeks after viral clearance.
The most commonly detected antibodies are against the N protein and the S protein.
Coronavirus neutralizing antibodies primarily target the trimeric spike (S) glycoproteins on the viral surface (Wang et al., 2020) and can change the course of infection in an infected individual by supporting virus clearance or protecting an uninfected host that is exposed to the virus (Prabakaran et al., 2009).
However, the antibody responses against SARS-CoV-2 remain poorly understood (Tang et al., 2020) and better understanding of how the viral coating triggers a healthy immune system’s recognition and neutralisation of the virus is critical for optimisation of diagnostic tests (Petherick, 2020).
It has been suggested that spike RBD may be a better target than N for diagnostic tests (Rosadas et al., 2020).
Applications:Suitable for use in ELISA and Western Blot.
Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Aliquots are stable for 12 months after receipt.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：100ug
Host：rabbit
Grade：Affinity Purified
Purity：Purified by Protein A affinity chromatography from serum.
Form：Supplied as a liquid in PBS, 0.09% sodium azide.
Specificity：Recognizes SARS-CoV-2 RBD. Does not cross-react in ELISA with HCoV-229E full-length spike protein
Isotype：IgG
Calc Applications Abbrev：E WB
Immunogen：Recombinant protein corresponding to aa319-541 from SARS-CoV-2 RBD, fused to His-Tag, expressed in HEK293 cells.
