Recombinant SARS-CoV-2 (2019-nCoV) Spike RBD protein

SDS-PAGE, Bioactivity

Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

An epidemic of acute respiratory syndrome in humans, which appeared in Wuhan, China in December 2019, was caused by a novel coronavirus (SARS-CoV-2). This disease was named as "Coronavirus Disease 2019" (COVID-19). This virus shares highly homological sequence with SARS-CoV, and causes acute, highly lethal pneumonia coronavirus disease 2019 (COVID-19) with clinical symptoms similar to those reported for SARS-CoV and MERS-CoV. The genome of this and other emerging pathogenic human CoVs encodes four major structural proteins [spike (S), envelope (E), membrane (M), and nucleocapsid (N)], approximately 16 nonstructural proteins (nsp1–16), and five to eight accessory proteins. Among them, the S protein plays an essential role in viral attachment, fusion, entry, and transmission. It comprises an N-terminal S1 subunit responsible for virus–receptor binding and a C-terminal S2 subunit responsible for virus–cell membrane fusion. S1 is further divided into an N-terminal domain (NTD) and a receptor-binding domain (RBD). SARS-CoV-2 and SARS-CoV bind angiotensin-converting enzyme 2 (ACE2) while MERS-CoV binds dipeptidyl peptidase 4 (DPP4), as receptors on the host cell expressing ACE2 (e.g., pneumocytes, enterocytes) or DPP4 (e.g., liver or lung cells including Huh-7, MRC-5, and Calu-3). During infection, CoV first binds the host cell through interaction between its S1-RBD and the cell membrane receptor, triggering conformational changes in the S2 subunit that result in virus fusion and entry into the target cell. Recombinant SARS-CoV-2 (2019-nCoV) Spike RBD, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques.

Liquid. In Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol

Virus

< 1 EU per 1ug of protein (determined by LAL method)

Ala

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