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Specifically recognize the SARS-CoV-2 Delta Spike RBD and ECD. No cross-reactivity with SARS-CoV-2 wild type, Alpha, Beta, Omicron BA.2.75 variant.. Has cross-reactivity in ELISA with: SARS-CoV-2 Delta (B.1.617.2) Spike S1+S2 trimer Protein; SARS-CoV-2 Delta (B.1.617.2) Spike RBD Protein; No cross-reactivity in ELISA with: SARS-CoV-2 Omicron (XBB.1.16) Spike S1+S2 trimer Protein; SARS-CoV-2 Omicron (XBB.1.5) Spike RBD Protein; SARS-CoV-2 Omicron (XBB.1.5) Spike S1+S2 trimer Protein; SARS-CoV-2 Omicron (XBB.1) Spike S1+S2 trimer Protein; SARS-CoV-2 Omicron (XBB) Spike RBD Protein; SARS-CoV-2 Omicron (BQ.1.1) Spike S1+S2 trimer Protein; SARS-CoV-2 Omicron (BQ.1.1)Spike RBD Protein; SARS-CoV-2 Omicron (BF.7) Spike S1+S2 trimer Protein; SARS-CoV-2 Omicron (BA.4.6/BF.7) Spike RBD Protein; SARS-CoV-2 Omicron (BA.4.6) Spike S1+S2 trimer Protein; SARS-CoV-2 Omicron (BA.2.75) Spike S1+S2 trimer Protein; SARS-CoV-2 Omicron (BA.2.75.2) Spike RBD Protein; SARS-CoV-2 Omicron (BA.2.75.2) Spike S1+S2 trimer Protein; SARS-CoV-2 Omicron (BA.4/BA.5/BA.5.2) Spike S1+S2 trimer Protein; SARS-CoV-2 Omicron (BA.4/BA.5/BA.5.2) Spike RBD Protein; SARS-CoV-2 Omicron (BA.2.75) Spike RBD Protein; SARS-CoV-2 Omicron (BA.2.3.20) Spike RBD Protein; SARS-CoV-2 Omicron (B.1.1.529) S1+S2 trimer Protein; SARS-CoV-2 Omicron (B.1.1.529) Spike RBD Protein; SARS-CoV-2 Alpha (B.1.1.7) Spike S1+S2 trimer Protein; SARS-CoV-2 Alpha (B.1.1.7) Spike RBD Protein; SARS-CoV-2 Beta (B.1.351) Spike S1+S2 trimer Protein; SARS-CoV-2 Beta (B.1.351, B.1.351.2, B.1.351.3) Spike RBD Protein; SARS-CoV-2 Spike S1+S2 (D614G) trimer Protein; SARS-CoV-2 Spike RBD Protein
The SARS-CoV-2 Delta Spike Protein RBD refers to the receptor-binding domain (RBD) of the spike (S) protein in the Delta variant of the SARS-CoV-2 virus, which is responsible for COVID-19. The RBD is a critical region within the S1 subunit of the spike protein that binds to the angiotensin-converting enzyme 2 (ACE2) receptor on human cells, facilitating viral entry. The Delta variant, first identified in India, possesses several mutations in the RBD that can enhance its binding affinity to the ACE2 receptor, potentially increasing the virus's transmissibility and partially evading immune responses. These mutations have significant implications for the effectiveness of vaccines and therapeutic antibodies, making it essential to monitor and adapt public health strategies accordingly.
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