£297.00
20 μg
2019-nCoV Spike protein RBD with was expressed in CHO cells using a C-terminal his tag.
Predicted Molecular Mass: The recombinant 2019-nCoV Spike protein RBD consists of amino acids 319-541 of the S1 subunit, receptor-binding domain (RBD) and predicts a molecular mass of 39 kDa.
2019-nCov amino acids: 319-541 of the S1 subunit, receptor-binding domain (RBD) (Gene Accession Number: MN908947)
Purity: >95 % as determined by densitometry.
Tag: His-tag
Endotoxin: <1.0 EU per μg protein as determined by the LAL method.
Activity: Measured by its binding ability in a functional ELISA. Immobilized human ACE2(19-740) protein (Fc tag) at 2μg/ml (100ul/well) can bind to 2019-nCoV spike protein RBD (His tag).
Expressed Host: CHO Cells
Species: 2019-nCoV
Concentration: 0.2μg/μl
Predicted Molecular Mass: The recombinant 2019-nCoV Spike protein RBD consists of amino acids 319-541 of the S1 subunit, receptor-binding domain (RBD) and predicts a molecular mass of 39 kDa.
2019-nCov amino acids: 319-541 of the S1 subunit, receptor-binding domain (RBD) (Gene Accession Number: MN908947)
Formulation: Recombinant protein stored in 50mM sodium phosphate, pH 7.5, 300mM NaCl, 150mM imidazole.
Storage: Store product at –70°C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favourable performance, avoid repeated handling and multiple freeze/thaw cycles.
Regulatory/Restrictions: For Research Use Only.
The severe acute respiratory syndrome related novel coronavirus SARSCoV-2 has caused the pandemic of the respiratory diseases (COVID-19) around the world in 2020. The spike glycoprotein (S) of coronavirus belongs to the type I transmembrane protein, which contains two subunits, S1 and S2, which is also known to be the key component to bind with host cells through the interaction with angiotensin-converting enzyme 2 (ACE2). A receptor binding domain (RBD) of S1 can recognise the cell surface receptor and the mutation of RBD could cause higher motility rate.