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nano-plotter™ micropipetting system  (Gesellschaft fur Silizium-Mikrosysteme)

 
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    Gesellschaft fur Silizium-Mikrosysteme nano-plotter™ micropipetting system
    Nano Plotter™ Micropipetting System, supplied by Gesellschaft fur Silizium-Mikrosysteme, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/nano_plotter/nano+plotter++micropipetting+system/pmc06166357-70-2-1
    Average 90 stars, based on 1 article reviews
    nano-plotter™ micropipetting system - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    other:

    Article Title: Associated measurement of fucosylated levels of AFP, DCP, and GPC3 for early diagnosis in hepatocellular carcinoma.
    Article Snippet: Approximately 100 pL of mouse monoclonal AFP antibody solution (1.25 mg/mL), mouse monoclonal prothrombin factor II antibody (2.5 mg/mL), mouse monoclonal glypican 3 antibody (1 mg/mL), and 10% BSA were spotted on the surfaces of slides in triplicates at 8°C with relative humidity of 50% by using the GeSiM Nano-PlotterTM Micropipetting System (Radeberg, Germany), as shown in Figure 1.

    Article Title: Analysis of serum alpha-fetoprotein (AFP) and AFP-L3 levels by protein microarray
    Article Snippet: The GeSiM Nano-PlotterTM Micropipetting System (Radeberg, Germany) was used to spot approximately 100 pL of mouse monoclonal AFP antibody solution (1.25 mg/mL) and 10% BSA on the surface of aldehyde-coated microscope slides (Shanghai Baiao Co., Shanghai, China) in triplicate ( ).



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    Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen <t>microarray.</t> ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.
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    Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen microarray. ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.

    Journal: Microbiology Spectrum

    Article Title: Nanobody engineering for SARS-CoV-2 neutralization and detection

    doi: 10.1128/spectrum.04199-22

    Figure Lengend Snippet: Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen microarray. ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.

    Article Snippet: Wild-type and variant SARS-CoV-2 RBD and spike S1 domains were biotinylated and arrayed as duplicate spots (0.1 ng per spot) in the wells of streptavidin-coated microtitration plates using a piezoelectric non-contact microarray dispenser (Nano-Plotter, GeSiM, Germany).

    Techniques: Binding Assay, Microarray, Construct, Fluorescence, Labeling, Standard Deviation, Variant Assay, Residue