Omicron rbd

Manufactured by Sino Biological

Sourced in United States, China

The Omicron RBD is a recombinant protein that corresponds to the receptor-binding domain (RBD) of the Omicron variant of the SARS-CoV-2 virus. It is a laboratory tool used for research purposes.

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Lab products found in correlation

Alpha rbd, by ACROBiosystems (1 mentions) Beta rbd, by ACROBiosystems (1 mentions) Delta rbd, by ACROBiosystems (1 mentions) Goat anti human igg hrp, by Jackson ImmunoResearch (1 mentions) Monophosphoryl lipid a mpl, by Merck Group (1 mentions) Omicron ba, by Sino Biological (1 mentions) Omicron ba 1, by Sino Biological (1 mentions) Prism 8, by GraphPad (1 mentions) Delta rbd, by Sino Biological (1 mentions)

Spelling variants of this product

Omicron (5 citations)

5 protocols using omicron rbd

SARS-CoV-2 RBD Protein Binding Assay

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RBD‐hFc protein (Prototype RBD SPD‐C5255; Alpha RBD, SPD‐C5253; Beta RBD SPD‐C5256; Delta RBD, SPD‐C525d, purchased from ACRO Biosystems; Omicron RBD, 40592‐V05H3 Sino Biological, purchased from Sino Biological) was diluted to 1 μg/ml with PBS buffer, then each concentration gradient was diluted twice; total of eight concentration gradients were set. 293T‐ACE2 cells were collected into flow tubes (2.5 × 10⁵ cells/tube). After washing once with PBS, the liquid was poured out for use. Add 100 μl of the RBD diluent in the previous step to the flow tube, respectively, and incubate at 37°C for 40 min. Add 2 ml of PBS to wash unbound proteins, and add 1 μl of Fc Tag flow antibody (BioLegend USA) to each tube for staining at 4°C for 30 min. The excess antibody was washed with PBS, and 500 μl of PBS solution was added for detection on the machine.

Yang H., Liu P., Zhang Y., Du T., Zhou Y., Lu S, & Peng X. (2022). Characteristic analysis of Omicron‐included SARS‐CoV‐2 variants of concern. MedComm, 3(2), e129.

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ELISA Quantification of RBD Antibodies

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ELISA was performed as previously described. (36 (link)) Recombinant WT RBD (in-house) and Omicron RBD (Catalog no. 40592-V08H121; Sino Biological) were coated in 1× PBS on MaxiSorp ELISA plates at 1 μg/mL concentration. After blocking with 1% BSA, plasma samples were plated in a 4-fold dilution series beginning at 1:100. Goat anti-human IgG-HRP was used to detect antibodies (catalog no.109-036-098; Jackson Immunoresearch Laboratories). Plates were developed using o-phenylenediamine dihydrochloride (OPD) substrate and stopped with 1 M hydrochloric acid. Absorbance was measured at 490 nm using a spectrophotometer (SpectraMax from Molecular Device). EC₅₀ was calculated using a nonlinear fit of transformed absorbance values.

Gupta S.L., Mantus G., Manning K.E., Ellis M., Patel M., Ciric C.R., Lu A., Turner J.S., O’Halloran J.A., Presti R.M., Joshi D.J., Ellebedy A.H., Anderson E.J., Rostad C.A., Suthar M.S, & Wrammert J. (2022). Loss of Pfizer (BNT162b2) Vaccine-Induced Antibody Responses against the SARS-CoV-2 Omicron Variant in Adolescents and Adults. Journal of Virology, 96(17), e00582-22.

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SARS-CoV-2 Variant Spike Protein Evaluation

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SARS-CoV-2 variant full length ectodomain spike with pre-fusion stabilizing mutations and receptor binding domain (RBD) proteins were purchased from Sino Biologicals (Wayne, PA, USA): Wuhan (40589-V08B1, S1+S2 ECD, 134.36 kDa, recombinant baculovirus), Delta (40589-V08B16, S1+S2 ECD, 134.20 kDa, recombinant baculovirus); Omicron BA.1 (40589-V08H26, S1+S2 ECD, 136.67 kDa, HEK293 Cells); Omicron BA.2 (S1+S2) (40589-V08H34); Omicron BA.4/5 (S1+S2) (40589-V08H32); Omicron XBB.1.5 (S1+S2) (40589-V08H45); Omicron RBD (40592-V08H121); human angiotensin-converting enzyme 2 (hACE2) protein (aa 1–740) fused to Fc tag (10108-H02H). Full-length ectodomain spike recombinant proteins (Wuhan, Delta, Omicron BA.1) displayed high levels of hACE2 receptor binding activity, with the Wuhan spike protein showing higher activity than Delta and Omicron BA.1 spike proteins, suggesting the integrity of the spike protein folding (Supplementary Figure S1). Wuhan RBD (NR-52366) was obtained from BEI (Biodefense and Emerging Infections Research Resources Repository). Monophosphoryl lipid A (MPL) and saponin QS-21 adjuvants were obtained from Sigma-Aldrich and Desert King (San Diego, CA, USA), respectively.

Liu R., Natekar J.P., Kim K.H., Pathak H., Bhatnagar N., Raha J.R., Park B.R., Guglani A., Shin C.H., Kumar M, & Kang S.M. (2024). Multivalent and Sequential Heterologous Spike Protein Vaccinations Effectively Induce Protective Humoral Immunity against SARS-CoV-2 Variants. Vaccines, 12(4), 362.

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Surface Heparin Competition Binding Assay

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Solution competition study between surface heparin and different soluble holothurian sulfated glycans (TgFucCS, TgSF, and UFH) was performed using SPR. In brief, protein samples SARS-CoV-2 S-Protein RBDs (wild type), mutants [L542 (delta) and omicron (BA.5 subvariant)], and coagulation (co)-factors (IIa, AT, and HCII) mixed with sulfated glycans (100 μg/mL) in HBS-EP buffer were injected over a heparin chip at a flow rate of 30 μL/min, respectively. After each run, the chip was regenerated with a 2 M NaCl injection. For each set of competition experiments on SPR, a control experiment (with only protein) was performed. Normalized binding of the proteins to surface heparin in the presence of different sulfated glycans was determined with respect to control values. This was calculated by dividing the obtained RU values of each experiment (using various glycans) by the control values. Each experiment was repeated in triplicates, and results were presented as the mean ± SD of the three experiments. SARS-CoV-2 S-protein RBD (wild type) and L542 mutant (delta) were provided by Prof. John Bates, University of Mississippi Medical Center. Omicron RBD (BA.2 subvariant) was purchased from Sino Biological Inc.

Dwivedi R., Farrag M., Sharma P., Shi D., Shami A.A., Misra S.K., Ray P., Shukla J., Zhang F., Linhardt R.J., Sharp J.S., Tandon R, & Pomin V.H. (2023). The Sea Cucumber Thyonella gemmata Contains a Low Anticoagulant Sulfated Fucan with High Anti-SARS-CoV-2 Actions against Wild-Type and Delta Variants. Journal of natural products, 86(6), 1463-1475.

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SARS-CoV-2 Protein Binding Assay

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ELISA plates were coated with SARS-CoV-2 protein including WT-S1, WT-NTD, WT-RBD, Delta-S1, Delta-RBD and Omicron-RBD (Sino Biological, China) at 4 °C overnight. Following washing with PBST (PBS with 0.5% (v/v) Tween 20), serial dilutions of testing antibodies starting at 5 μg/mL were added to each well and incubated at 37 °C for 30 min. After washing with PBST, horseradish peroxidase (HRP)-conjugated anti-human IgG Fc specific antibody (Sigma, USA) was added at the dilution of 1:2000 and incubated at 37 °C for 30 min. The absorbance was detected at 450 nm. The data were analyzed using GraphPad Prism 8.0.

Li X., Pan Y., Yin Q., Wang Z., Shan S., Zhang L., Yu J., Qu Y., Sun L., Gui F., Lu J., Jing Z., Wu W., Huang T., Shi X., Li J., Li X., Li D., Wang S., Yang M., Zhang L., Duan K., Liang M., Yang X, & Wang X. (2022). Structural basis of a two-antibody cocktail exhibiting highly potent and broadly neutralizing activities against SARS-CoV-2 variants including diverse Omicron sublineages. Cell Discovery, 8, 87.

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