Specifications
Species Reactivity
SARS-CoV-2
Immunogen
Recombinant SARS-CoV-2 Spike RBD-mFc Protein
Applications
Application Notes
ELISA: 0.5-1 ug/mL
Target
Alternative Names
SARS-CoV-2; coronavirus; SARS-CoV-2 spike 1; SARS-CoV-2 spike protein; SARS-CoV-2 S1; SARS-CoV-2 RBD; SARS-CoV-2 spike RBD
Citations
Publication ()
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A Novel Non-Destructive Rapid Tool for Estimating Amino Acid Composition and Secondary Structures of Proteins in Solution
Altangerel N, Neuman BW, Hemmer PR, Yakovlev VV, Sokolov AV, Scully MO
Applications: Unspecified application
Reactive species: Unspecified reactive species
"Abstract: Amino-acid protein composition plays an important role in biology, medicine, and nutrition. Here, a groundbreaking protein analysis technique that quickly estimates amino acid composition and secondary structure across various protein sizes, while maintaining their natural states is introduced and validated. This method combines multivariate statistics and the thermostable Raman interaction profiling (TRIP) technique, eliminating the need for complex preparations. In order to validate the approach, the Raman spectra are constructed of seven proteins of varying sizes by utilizing their amino acid frequencies and the Raman spectra of individual amino acids. These constructed spectra exhibit a close resemblance to the actual measured Raman spectra. Specific vibrational modes tied to free amino and carboxyl termini of the amino acids disappear as signals linked to secondary structures emerged under TRIP conditions. Furthermore, the technique is used inversely to successfully estimate amino acid compositions and secondary structures of unknown proteins across a range of sizes, achieving impressive accuracy ranging between 1.47% and 5.77% of root mean square errors (RMSE). These results extend the uses for TRIP beyond interaction profiling, to probe amino acid composition and structure."
Article snippet: Mouse Anti-SARS CoV-2 Spike Neutralizing IgG2b (clone NN68) purchased from the Creative Diagnostics.
Label-free drug interaction screening via Raman microscopy
Narangerel Altangerel, Benjamin W Neuman, Philip R Hemmer, Vladislav V Yakovlev, Navid Rajil, Zhenhuan Yi, Alexei V Sokolov, Marlan O Scully
Proc Natl Acad Sci U S A2023 JulPubMed ID: 37463207Read Article
Applications: Neut
Reactive species: SARS-CoV-2
"Abstract: Development of a simple, label-free screening technique capable of precisely and directly sensing interaction-in-solution over a size range from small molecules to large proteins such as antibodies could offer an important tool for researchers and pharmaceutical companies in the field of drug development. In this work, we present a thermostable Raman interaction profiling (TRIP) technique that facilitates low-concentration and low-dose screening of binding between protein and ligand in physiologically relevant conditions. TRIP was applied to eight protein-ligand systems, and produced reproducible high-resolution Raman measurements, which were analyzed by principal component analysis. TRIP was able to resolve time-depending binding between 2,4-dinitrophenol and transthyretin, and analyze biologically relevant SARS-CoV-2 spike-antibody interactions. Mixtures of the spike receptor-binding domain with neutralizing, nonbinding, or binding but nonneutralizing antibodies revealed distinct and reproducible Raman signals. TRIP holds promise for the future developments of high-throughput drug screening and real-time binding measurements between protein and drug."
Article snippet: The receptor-binding domain (RBD) (residues 319 to 541) of the SARS CoV-2 spike (S) protein (*) was purchased from *, Human Anti-SARS CoV S IgG1 (*) was purchased from the *, and Mouse Anti-SARS CoV-2 Spike Neutralizing IgG2b (clone NN68) was purchased from the Creative Diagnostics. 
Figure 1. Raman spectra of antibodies (black), their SpA mixes (blue) and SpA (pink) with their SEs (shaded).
Design and characterization of chimeric Rabies-SARS-CoV-2 virus-like particles for vaccine purposes
Ernesto Garay, Diego Fontana, Javier Villarraza, Antonela Fuselli, Agustina Gugliotta, Sebastián Antuña, Belén Tardivo, María Celeste Rodríguez, Victoria Gastaldi, Juan Manuel Battagliotti, Diego Alvarez, Eliana Castro, Juliana Cassataro, Natalia Ceaglio, Claudio Prieto
Appl Microbiol Biotechnol2023 JunPubMed ID: 37126083Read Article
Applications: FC
Reactive species: Unspecified reactive species
"Abstract: Due to the high number of doses required to achieve adequate coverage in the context of COVID-19 pandemics, there is a great need for novel vaccine developments. In this field, there have been research approaches that focused on the production of SARS-CoV-2 virus-like particles. These are promising vaccine candidates as their structure is similar to that of native virions but they lack the genome, constituting a biosafe alternative. In order to produce these structures using mammal cells, it has been established that all four structural proteins must be expressed. Here we report the generation and characterization of a novel chimeric virus-like particle (VLP) that can be produced by the expression of a single novel fusion protein that contains SARS-CoV-2 spike (S) ectodomain fused to rabies glycoprotein membrane anchoring region in HEK293 cells. This protein is structurally similar to native S and can autonomously bud forming enveloped VLPs that resemble native virions both in size and in morphology, displaying S ectodomain and receptor binding domain (RBD) on their surface. As a proof of concept, we analyzed the immunogenicity of this vaccine candidate in mice and confirmed the generation of anti-S, anti-RBD, and neutralizing antibodies. KEY POINTS: • A novel fusion rabies glycoprotein containing S ectodomain was designed. • Fusion protein formed cVLPs that were morphologically similar to SARS-CoV-2 virions. • cVLPs induced anti-S, anti-RBD, and neutralizing antibodies in mice."
Article snippet: Seventy-two hpt, cells were trypsinized and washed with PBS, and then they were incubated with either an anti-SARS-CoV-2 RBD monoclonal antibody (mAb) (NN68, Creative Diagnostics) diluted 1/500 in PBS, or a convalescent serum diluted 1/200 in PBS for 45 min at RT. 
Figure 1. Chimeric protein expression analysis by flow cytometry
COA
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