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SARS-CoV-2 Variants Research Reagents

The Omicron variant has been designated as a variant of concern (VOC) by the WHO. Omicron is now designated as the most contagious variant with at least twice the spreading speed compared to the Delta variant according to scientists in southern Africa. Omicron variant spike protein includes mutations, deletions, and insertions, which are related to transmissibility increase, immune escape, and resistance to monoclonal antibody treatments.

To enable a proteomic analysis of SARS-CoV-2 protein expression, ProSci R&D has created SARS-CoV-2 point mutation-specific antibodies, for Omicron (9793, 9805, PM-9375, 9091), Delta (9689, 9463, PM-9677), Gamma (9573, PM-9590), and Alpha (9359, PM-9371) variants.

ProSci further offers Omicron variant recombinant proteins, including Spike Trimer (21-845), Spike S1 (21-846, 95-129) and RBD proteins (95-128, 21-801, 21-844) with His-Avi tag, and Nucleocapsid protein (21-850). We also offer Delta variant Spike S1 (95-127) and RBD (95-126, 21-831) proteins with His-Avi tag. These are proteomics tools to interrogate viral and VLP expression.

SARS-CoV-2 variants reagents from ProSci

Select Your SARS-CoV-2 Variant of Concern

References

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  • Gamage, Akshamal M., Kai Sen Tan, Wharton O. Y. Chan, Jing Liu, Chee Wah Tan, Yew Kwang Ong, Mark Thong, et al. 2020. “Infection of Human Nasal Epithelial Cells with SARS-CoV-2 and a 382-Nt Deletion Isolate Lacking ORF8 Reveals Similar Viral Kinetics and Host Transcriptional Profiles.” PLoS Pathogens 16 (12): e1009130.
  • Gu, Hongjing, Qi Chen, Guan Yang, Lei He, Hang Fan, Yong-Qiang Deng, Yanxiao Wang, et al. 2020. “Adaptation of SARS-CoV-2 in BALB/c Mice for Testing Vaccine Efficacy.” Science 369 (6511): 1603–7.
  • Hoffmann, Markus, Hannah Kleine-Weber, and Stefan Pöhlmann. 2020. “A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells.” Molecular Cell 78 (4): 779–84.e5.
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  • McCarthy, Kevin R., Linda J. Rennick, Sham Nambulli, Lindsey R. Robinson-McCarthy, William G. Bain, Ghady Haidar, and W. Paul Duprex. 2020. “Natural Deletions in the SARS-CoV-2 Spike Glycoprotein Drive Antibody Escape.” Microbiology. bioRxiv.
  • Peacock, Thomas P., Daniel H. Goldhill, Jie Zhou, Laury Baillon, Rebecca Frise, Olivia C. Swann, Ruthiran Kugathasan, et al. 2020. “The Furin Cleavage Site of SARS-CoV-2 Spike Protein Is a Key Determinant for Transmission due to Enhanced Replication in Airway Cells.” Cold Spring Harbor Laboratory. https://doi.org/10.1101/2020.09.30.318311.
  • Starr, Tyler N., Allison J. Greaney, Sarah K. Hilton, Daniel Ellis, Katharine H. D. Crawford, Adam S. Dingens, Mary Jane Navarro, et al. 2020. “Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding.” Cell 182 (5): 1295–1310.e20.
  • Zhu, Yunkai, Fei Feng, Gaowei Hu, Yuyan Wang, Yin Yu, Yuanfei Zhu, Wei Xu, et al. 2020. “The S1/S2 Boundary of SARS-CoV-2 Spike Protein Modulates Cell Entry Pathways and Transmission.” Cold Spring Harbor Laboratory. https://doi.org/10.1101/2020.08.25.266775.