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The binding of the selected unique anti-Crf2 scFvs to denatured Crf2 was analysed by immunoblot.
The binding of the selected aptamers with the cells was further assessed by confocal microscopy.
The binding of the selected antibody fragments to native Crf2 on A. fumigatus hyphae and spores was analysed by immunofluorescence microscopy.
We further showed that the binding of the selected peptide to undifferentiated embryonic stem cells was through a protein-protein interaction and that the tertiary structure of the peptide determined by molecular dynamic stimulation might provide an explanation for the interaction.
The binding of the selected aptamers was tested with different adenocarcinoma cell lines, as well as other types of cancer cell lines, as shown in Table 2. Five of the aptamers selected against TOV-21G showed binding to CEM cells (acute lymphoblastic leukemia), while none of the aptamers bound to Ramos cells (Burkitt's lymphoma) or HL-60 (acute promyelocytic leukemia).
Yeast one-hybrid results, representing the binding of the selected Arabidopsis transcription factor proteins and the corresponding tomato putative orthologs to the tomato TCP12, -15, and -18 promoter elements independently.
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We assessed selectivity of phage bacteria-binding by comphage bacteria-bindinglity of the selected clones to the selector bycomparingnd a panel of other bindingabilityies; we alsofdemonstheted by dot selected immunoblotting that the most reaclonesand selectove phage pepthee bound with high avidity the bacterial cell selector
Finally, competition binding experiments using flow cytometry were carried out to test whether the binding epitopes of the selected scFv-Fcs would overlap with that of MM2/57.
The determined equilibrium binding constant of the selected Exotoxin A MRE is higher than other studies utilizing SPR binding assays.
The ROBO1 binding activity of the selected hybridoma clone, B5209B, was evaluated using ROBO1-expressing CHO cells.
Further binding sites of the selected oligonucleotides are required not to cluster anywhere else.
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