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Method: A lactam bridge-cyclized H-Cys-Ahx-βAla3-c[Lys4-Glu-His-D-Phe-Arg-Trp-Glu10]-Arg11-Pro-Val-NH2 (NandNS2) and the corresponding linear H-Cys-Ahx-βAla-Nle-Asp-His-D-Phe-Arg-Trp-Gly-NH2 (NAP-NS1) peptide were synthetized, characterized by ESI-MS spectroscopy and their MC1R binding affinity were determined in B16/F10 melanoma cells.
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HER2 binding affinity was determined in saturation radioligand binding assays using SKBR-3 cells (1.3 × 106 HER2/cell).
Belatacept was labeled with indium-111, and the binding affinity was determined with CD80/CD86-positive CD80/CD86-positive
In this study, we found three aptamers, and binding affinity was determined by fluorescently labeled aptamers.
LXY30-FITC and S-LXY30-FITC were incubated with U-87MG cells, and the binding affinity was determined by flow cytometry analysis.
The binding affinity was determined for two of the six ligands, F152 and F090.
The binding affinity was determined by plotting the binding response at equilibrium against the concentration of rCR2 and fitting a Langmuir binding isotherm (Figure 3b).
Instead the overall binding affinity is determined cooperatively by nucleotides in a region.
The binding affinity was determined using the continuous variation method [20].
Their integrin αvβ3/αvβ5 binding affinity was determined in a displacement assay against I-echistatin bound to U87MG glioma cells.
The binding affinity was determined to be in the submicromolar range similar to that observed for binding of native toxin to cells (Van Itallie et al. 2008).
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