2019-nCoV Spike RBD+SD1
19Cov-S13019Cov-S130
$350.00 – $1,500.00
Protein Name | 2019-nCoV Spike RBD + SD1 |
Catalog Number | 19Cov-S13019Cov-S130 |
Purity | 90% or above |
Protein Construction | A DNA sequence encoding the SARS-CoV-2 (2019-nCoV) spike protein receptor binding domain and subdomain (Arg319-Ser591) |
Endotoxin | <0.1 EU per ug of protein as determined by LAL method |
Origin Species | 2019-nCoV Spike RBD + SD1 |
Expression Host | HEK293F |
Protein type | Recombinant |
Purification tag | C-terminal 6xHis-tag |
Molecule Mass | Predicted molecular weight 31.8 KD |
Formulation | PBS |
Regulation restrictions | For research use only |
Shipping | Recombinant proteins are provided as frozen liquid and will be shipped out with dry ice. |
Stability and storage | The protein is stable in a liquid state at -70℃ for 12 months. Avoid repeated freeze-thaw cycles. |
Additional information
Size | 100µg, 1mg |
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Background information
The SARS-CoV-2 (2019-nCoV) Spike RBD (receptor binding domain) has been identified as the key viral element allowing the virus docking to the target cells. RDB is recognized by the ACE2 surface membrane receptor [1-3]. RBD is a candidate for subunit prophylactic vaccines against SARS-CoVs [4, 5]. RBD is also at the center of therapeutic approaches, such as the development and testing of small peptide inhibitors or soluble ACE2 to block the SARS-CoV-2 entry into target cells [6].
References:
- Li F., 2016. Structure, function, and evolution of coronavirus spike proteins. Annu. Rev. Virol. 3:237-261.
- Li F. et al., 2005. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science. 309:1864-1868.
- Walls A.C. et al., 2020. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell. 181(2):281-292.e6.
- Wang N. et al., 2020. Subunit vaccines against emerging pathogenic human coronaviruses. Front. Microbiol. 11:298. DOI: 10.3389/fmicb.2020.00298.
- Padron-Regalado E., 2020. Vaccines for SARS-CoV-2: Lessons from other coronavirus strains. Infect. Dis. Ther. DOI: 10.1007/s40121-020-00300-x.
- Monteil V.et al., 2020. Inhibition of SARS-CoV-2 infections in engineered human tissues using clinical-grade soluble human ACE2. Cell. 181:1-9.
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