Recombinant SARS-CoV-2 RBD Protein, His-tagged
Welcome! For price inquiries, please feel free to contact us through the form below. We will get back to you as soon as possible.
|Product Overview :||Purified recombinant fusion protein that includes the RBD of SARS-CoV-2 Spike protein (S-Protein) and Virion Surface Domain of Membrane Protein (M-protein) with C-terminal HIS-tag was expressed in HEK293.|
|Bio-activity :||Binding of SARS-CoV-2 S-M Fusion Protein to Human ACE2: 2 ug/ml of SARS-CoV-2 Spike and Membrane viral fusion protein (gel insert) was immobilized on an ELISA plate and its ability to bind to Human ACE2 was measured. The EC50 was between 10-20 ng/ml.|
|Molecular Mass :||34 kDa|
|AA Sequence :||MALWIDRMQL LSCIALSLAL VTNSAKGIYQ TSNFRVQPTE SIVRFPNITN LCPFGEVFNA TRFASVYAWN RKRISNCVAD YSVLYNSASF STFKCYGVSP TKLNDLCFTN VYADSFVIRG DEVRQIAPGQ TGKIADYNYK LPDDFTGCVI AWNSNNLDSK VGGNYNYLYR LFRKSNLKPF ERDISTEIYQ AGSTPCNGVE GFNCYFPLQS YGFQPTNGVG YQPYRVVVLS FELLHAPATV CGPKKSTNLV KNKCVNFNFN GLTGTGVLTE SNKKFLGGGS GGGSMADSNG TITVEELKKH HHHHH|
|Purity :||> 90% as determined by SDS-PAGE and Coomassie blue staining|
|Stability :||Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.|
|Storage :||Store at -80 centigrade.|
|Concentration :||>50 μg/mL as determined by Bradford protein assay method.|
|Storage Buffer :||PBS, 10% glycerol.|
|Binding activity measured by ELISA :||
Immobilized SARS-CoV-2 Spike Membrane Fusion Protein (RBD of S-Protein and Virion Surface Domain of M-Protein with His Tag at 2 µg/mL (100 µL/well) can bind to Human ACE2 Fc Tag, the EC50 of the human ACE2 protein is 10-20 ng/ml.
|ELISA plates were coated with anti-HIS as capture antibody :||
5ng of HIS-tagged SARS-Cov-2 Spike-membrane recombinant fusion protein was then added as substrate. Human anti-S antibody against SARS-Cov-2 Spike protein RBD was applied for detection. HRP assay was used for readout. Coating with anti-DDK antibody was served as negative control.