Recombinant SARS-CoV Spike RBD protein

Measured by its binding ability in a functional ELISA with Human ACE-2 (CAT# ATGP3963)

RVVPSG DVVRFPNITN LCPFGEVFNA TKFPSVYAWE RKKISNCVAD YSVLYNSTFF STFKCYGVSA TKLNDLCFSN VYADSFVVKG DDVRQIAPGQ TGVIADYNYK LPDDFMGCVL AWNTRNIDAT STGNYNYKYR YLRHGKLRPF ERDISNVPFS PDGKPCTPPA LNCYWPLNDY GFYTTTGIGY QPYRVVVLSF ELLNAPATVC GPKL

Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV), Middle Eastern Respiratory Syndrome Coronavirus (MERS-CoV), and the recently identified novel Coronavirus (SARS-CoV-2) belong to the Coronaviridae family, genus Betacoronavirus, that has been related to important epidemiological outbreaks. SARS-CoV emerged in 2003 as a significant threat to human health. SARS-CoV has four structural proteins, known as the S (spike), E (envelope), M (membrane), and N (nucleocapsid) proteins. The spike protein, responsible for allowing the virus to attach to and fuse with the membrane of a host cell and is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity. It attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. A metallopeptidase, angiotensin-converting enzyme 2 (ACE-2), has been identified as a functional receptor for SARS-CoV through interaction with a receptor binding domain (RBD) located at the C-terminus of S1 subunit. Recombinant SARS-CoV spike RBD protein fused to His-tag at C-terminus, was expressed in HEK293 cell and purified by using conventional chromatography techniques.

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

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

Kukla M., et al, (2020) J Clin Med. 9:1420.; ; Ayouba A., et al, (2020) J Clin Virol. 129:104521.; ; Tortorici, M.A. and D. Veesler (2019). Adv. Virus Res. 105:93-116.; ; Li F, et al, (2005) Science. 309:1864-1868.; ; Struck AW, et al, (2012) Antiviral Res. 94:288-296.

Asp