SARS-CoV-2 S Protein RBD (Biotinylated, Omicron, B.1.1.529, HEK293, His-Avi)

The SARS-Cov-2 S glycoprotein is a SARS-Cov-2 S glycoprotein. The amino acid sequence 1261-1267a.a of the SARS-Cov-2 S glycoprotein is transmembrane. The SARS-Cov-2 S glycoprotein is a highly glycosylated trimer, each of which consists of 1260 amino acids (residues 14-1273), divided into four structural domains: the n-terminal domain (NTD), the c-terminal domain (CTD, also known as the receptor-binding domain, RBD), and two subdomains (SD1 and SD2). SARS-CoV-2 S Protein RBD (Biotinylated, Omicron, B.1.1.529, HEK293, His-Avi) is the recombinant Virus-derived SARS-CoV-2 S protein RBD, expressed by HEK293 , with C-Avi, C-His labeled tag.

SARS-Cov-2 is a enveloped positive-sense single-stranded RNA virus that causes COVID-19.
SARS-CoV-2 possesses four structural proteins, namely the envelope protein (E), spike or surface glycoprotein (S), membrane protein (M), and nucleocapsid protein (N).
The SARS-Cov-2 S glycoprotein is located on the exterior of the viral particle, giving the coronavirus its crown-like appearance.
The SARS-Cov-2 S glycoprotein can mediate the attachment and entry of viral particles into host cells and is an important target for vaccine development, antibody therapy, and antigen-based diagnostic esting^{[1][2][3][4][5]}.

Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2 S1 at 2 μg/mL (100 μL/well) on the plate can bind human ACE2 (HY-P7443). The ED₅₀ for this effect is 12.48 ng/mL.

Virus

HEK293

C-Avi;C-His

YP_009724390 (R319-F541)

43740568  [NCBI]

Full Length of SARS-CoV-2_Spike_S1_RBD

Approximately 28.64 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Solution.

Supplied as a 0.22 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

N/A.

Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.

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  [2]. Lorenz P, et al. A linear B-cell epitope close to the furin cleavage site within the S1 domain of SARS-CoV-2 Spike protein discriminates the humoral immune response of nucleic acid- and protein-based vaccine cohorts. Front Immunol. 2023 May 5;14:1192395.  [Content Brief]

  [3]. Wang X, et al. Evaluating the effect of SARS-CoV-2 spike mutations with a linear doubly robust learner. Front Cell Infect Microbiol. 2023 Apr 19;13:1161445.  [Content Brief]

  [4]. Bestle D, et al. TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells. Life Sci Alliance. 2020 Jul 23;3(9):e202000786.  [Content Brief]

  [5]. Duan L, et al. The SARS-CoV-2 Spike Glycoprotein Biosynthesis, Structure, Function, and Antigenicity: Implications for the Design of Spike-Based Vaccine Immunogens. Front Immunol. 2020 Oct 7;11:576622.  [Content Brief]