SARS-CoV-2 Neutralization Antibody ELISA Kit(Quantitative) (E-EL-E608)

This ELISA kit uses Competitive-ELISA as the method to qualitatively detect the Anti-SARS-CoV-2 Neutralization Antibody in the sample. _x000D_ The micro ELISA plate provided in this kit is pre-coated with recombinant human ACE2. During the reaction, the SARS-CoV-2 Neutralization Antibody in the pretreated samples or controls competes with a fixed amount of human ACE2 on the solid phase supporter for sites on the Horseradish peroxidase (HRP) conjugated recombinant SARS-CoV-2 RBD fragment (HRP-RBD). After 37℃ incubation, the unbound HRP-RBD as well as any HRP-RBD bound to non-Neutralization antibody will be captured on the plate and eventually form the ACE2-RBD-HRP complex, while the circulating neutralization antibodies HRP-RBD complexes remain in the supernatant and are removed during washing. Then a TMB substrate solution is added to each well. The enzyme-substrate reaction is terminated by the addition of stop solution and the color change is measured spectrophotometrically at a wavelength of 450 nm ± 2 nm. Compared with the inhibition ratio to judge whether SARS-CoV-2 Neutralization Antibody exists in the tested samples or not.

SARS-CoV-2, which causes the global pandemic coronavirus disease 2019 (Covid-19), belongs to a family of viruses known as coronaviruses that are commonly comprised of four structural proteins: Spike protein (S), Envelope protein (E), Membrane protein (M), and Nucleocapsid protein (N) . SARS-CoV-2 Spike Protein (S Protein) is a glycoprotein that mediates membrane fusion and viral entry. The S protein is homotrimeric, with each ~180-kDa monomer consisting of two subunits, S1 and S2. In SARS-CoV-2, as with most coronaviruses, proteolytic cleavage of the S protein into the S1 and S2 subunits is required for activation. The S1 subunit is focused on attachment of the protein to the host receptor while the S2 subunit is involved with cell fusion. The S protein of SARS-CoV-2 shares 75% and 29% amino acid (aa) sequence identity with the S protein of SARS-CoV-1 and MERS, respectively.The S Protein of the SARS-CoV-2 virus, like the SARS-CoV-1 counterpart, binds Angiotensin-Converting Enzyme 2 (ACE2), but with much higher affinity and faster binding kinetics through the receptor binding domain (RBD) located in the C-terminal region of S1. Based on structural biology studies, the RBD can be oriented either in the up无standing or down无lying state with the up无standing state associated with higher pathogenicity. Polyclonal antibodies to the RBD of the SARS-CoV-2 protein have been shown to inhibit interaction with the ACE2 receptor, confirming RBD as an attractive target for vaccinations or antiviral therapy. It has been demonstrated that the S Protein can invade host cells through the CD147无EMMPRIN receptor and mediate membrane fusion. A SARS-CoV-2 variant carrying the S protein aa change D614G has become the most prevalent form in the global pandemic and has been associated with greater infectivity and higher viral load .