SARS CoV-2 Spike B.1.351 Mutation RBD domain

SARS CoV-2 Spike B.1.351 Mutation RBD domain
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All viruses undergo fast mutations and adept quickly to the countermeasures that the immune... more
Product information "SARS CoV-2 Spike B.1.351 Mutation RBD domain"
Product Type: Mutant Spike Protein
Protein Sequence: RB Domain
All viruses undergo fast mutations and adept quickly to the countermeasures that the immune systems creates against them. SARS-CoV-2 of the COVID-19 pandemic is no exception here. During the pandemic multiple mutant strains arose. To help the science combat these mutants Cube Biotech offers the RB-Domains of these mutant SPIKE proteins.

That is the full Receptor-Binding Domain of the SPIKE surface protein SARS-CoV-2 of the mutant strain B.1.351, also commonly known as the "SA / South Africa mutant". Its individual mutations are listed in the "features" table below.
Further SPIKE related products by Cube Biotech include:
    1. Full-length & active SPIKE protein of mutant Strain B.1.351 stabilized in LMNG
    2. The RB-Domain of SPIKE mutant strain B.1.1.7, also known as the "UK mutant"
    3. The RB-Domain of SPIKE mutant strain P.1, also known as the "Brazil mutant"
    4. The "original" SPIKE protein in LMNG.
    5. Anti-SPIKE antibodies

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Uk mutant SPIKE in SDS page, westernblotFigure 1: Size, purity and oligomerization state of CoV-2 spike protein RBD domain assessed by SDS-PAGE, Western Blot using an anti-His antibody.

Features

Alternative names SPIKE_SARS2 Spike glycoprotein
UniProt number P0DTC2
Protein class Single span transmembrane protein
Organism Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
Sequence RBD domain (aa 319 – 537), K417N, E484K, N501Y, C-terminal His-tag
Affinity tag C-terminal His-tag
Expression Host Hek293 Expi cells
Size 225 amino acids (including His-tag)
25491 Da
Buffer composition 20 mM Hepes pH 7.5; 150 mM NaCl
Function host cell surface receptor binding; fusion of virus membrane with host endosome membrane
Purity (SDS-PAGE) >98% as determined by SDS-PAGE, see Fig. 1 A and B
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