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1دورية أكاديمية
المؤلفون: Shih-Wei Wu, Ying-Ju Chen, Yu-Wen Chang, Cheng-Yang Huang, Biing-Hui Liu, Feng-Yih Yu
مصطلحات موضوعية: Biophysics, Biochemistry, Microbiology, Molecular Biology, Biotechnology, Ecology, Cancer, Infectious Diseases, Chemical Sciences not elsewhere classified, SARS-CoV-2, Oligonucleotide aptamer, Monoclonal antibody, Hybrid enzyme-linked aptamer-antibody sandwich assay, Hybrid lateral flow strip
الوصف: Additional file 1: Table S1. Comparison of commercial antibodies specific SARS-CoV-2 N protein using iELISA. Table S2. Comparison of commercial ELISA kit for SARS-CoV-2 antigen detection. Table S3. Comparison of commercial rapid test strip for SARS-CoV-2 antigen detection. Table S4. Performance indicators of hybrid lateral flow strip for infected and healthy volunteers. Fig. S1. Western blotting analysis of expression SARS-CoV-2 N protein using commercial anti-SARS-CoV-2 N protein antibodies. Fig. S2. The stability analysis of (A) the hybrid ELAAA was conducted throughout its storage period under 4 °C. The results represent the mean ± SD of absorbance value obtained from three independent replicates. (B-C) the hybrid-LFS was conducted throughout its storage period under vacuum packaging. The results represent the mean ± SD of test line intensity (RLU) obtained from three independent replicates. Fig. S3. Optimization of the Hybrid-LFA. (A) Comparison of the pH value of conjugation buffer. Hybrid-LFA conditions include 20 nm gold nanoparticles with 150 µg of mAb in this evaluation. (B) Comparison of the particle size of the gold nanoparticle. This assessment involves conjugation buffer (pH 5.5) and 150 µg of mAb under hybrid-LFA conditions. (C) Comparison of the quantity of antibodies on the surfaces of gold nanoparticles. The examination is conducted using conjugation buffer (pH 5.5) and 40 nm gold nanoparticles within hybrid-LFA settings. All compared groups utilize samples containing 100 ng/mL SARS-CoV-2 N protein and 0 ng/mL SARS-CoV-2 N protein.
الإتاحة: https://doi.org/10.6084/m9.figshare.24934072.v1Test
https://figshare.com/articles/journal_contribution/Additional_file_1_of_Novel_enzyme-linked_aptamer-antibody_sandwich_assay_and_hybrid_lateral_flow_strip_for_SARS-CoV-2_detection/24934072Test -
2
المؤلفون: Feng-Yih Yu, Fun S. Chu
المصدر: Food and Agricultural Immunology. 11:297-306
مصطلحات موضوعية: Fumonisin B1, biology, medicine.drug_class, Toxin, medicine.medical_treatment, Immunology, Hemocyanin, Monoclonal antibody, medicine.disease_cause, Horseradish peroxidase, Molecular biology, Isotype, Microbiology, chemistry.chemical_compound, chemistry, Cell culture, biology.protein, medicine, Antibody, Agronomy and Crop Science, Food Science
الوصف: Monoclonal antibodies (mAb) against fumonisin B1 (FmB1) were produced from a stable hybridoma cell line, 9C11E6, generated by the fusion of P3/NS-1/1-AG4-1 myeloma cells with spleen cells isolated from a BALB/c mouse immunized with FmB1-keyhole limpet hemocyanin. The 9C11E6 mAb belong to the immunoglobulin G1 (kappa chain) isotype with the highest specificity for FmB3. A direct competitive enzyme-linked immunosorbent assay (dc-ELISA) and an indirect competitive ELISA (idc-ELISA) were established for antibody characterization and toxin analysis. The concentrations causing 50% inhibition (IC 50 ) of binding of FmB1- horseradish peroxidase with the antibodies by FmB1, FmB2, and FmB3 in the dc-ELISA were found to be 29.1, 17.5, and 4.1 ng ml -1 , respectively. The IC 50 values of the binding of 9C11E6 mAb to the solid-phase FmB1-ovalbumin by free FmB1, FmB2, and FmB3 in the idcELISA were found to be 20.1, 13.2, and 16.8 ng ml -1 , respectively. The average recovery of FmB1 (50-2000 ng g -1 ) added to cornmeal...
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::6f813416b0e52aaa111381fa23b3b325Test
https://doi.org/10.1080/09540109999681Test
