Name : SARS Spike RBD Protein

Product Source :
Recombinant SARS Spike RBD Protein is expressed from HEK293 with His tag and Avi tag at the C-Terminus. It contains Arg306-Phe527.[Accession | P59594]

Molecular Weight :
The protein has a predicted MW of 27.9 kDa. Due to glycosylation, the protein migrates to 36-46 kDa based on Tris-Bis PAGE result.

Endotoxin Level :
Less than 1EU per μg by the LAL method.

Purity :
> 95% as determined by Tris-Bis PAGE> 95% as determined by HPLC

Formulation :
Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.

Reconstitution :
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.

Storage and Stability :
-20 to -80°C for 12 months as supplied from date of receipt. -80°C for 3-6 months after reconstitution. 2-8°C for 2-7 days after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.

Product Concentration :
Tris-Bis PAGE SARS Spike RBD on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. SEC-HPLC The purity of SARS Spike RBD is greater than 95% as determined by SEC-HPLC. ELISA Data Immobilized SARS Spike RBD, His Tag at 2μg/ml (100μl/well) on the plate. Dose response curve for Human ACE2, hFc Tag with the EC50 of 39.0ng/ml determined by ELISA.

Background :
The spike protein (S) of coronavirus (CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Synonyms :
S protein RBD; S glycoprotein RBD; Spike protein RBD

References & Citations :
(1)Belouzard S , Chu V C , Whittaker G R. Activation Of The Sars Coronavirus Spike Protein Via Sequential Proteolytic Cleavage At Two Distinct Sites[J]. Proceedings of the National Academy of Sciences of the United States of America, 2009, 106(14):5871-5876.

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