Introduction to Pd L1 Aptamer
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The PD-L1 Antibody on the surface of gold chip and the PD-L1 aptamer on MNOM@AgNCs could realize dual selective recognition of PD-L1, providing the specificity of the sensor and reducing non-specific binding.
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In this study, we isolated PD-L1 aptamers using a combination method, named Modular-SELEX (systematic evolution of ligands by exponential enrichment), which includes three sequentially performed modules: the affinity module, the specificity module, and the compatibility module.
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The glycosylation of exosomal PD-L1 (exoPD-L1) was imaged in situ using intramolecular fluorescence resonance energy transfer (FRET) between fluorescent PD-L1 aptamers bound on exoPD-L1 and fluorescent tags on glycans introduced via metabolic glycan labeling.
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The reported PD-L1 aptamers and antibodies are both extracellular region binding molecules with the overlapping binding sites, which seriously limit with the construction of biosensor.
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In the absence of PD-L1°C the PD-L1 aptamer is absorbed on the surface of graphene oxide modified magnetic nanoparticles °8rGO-MNPS°9 and leading to effective fluorescence quenching.
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PD-L1 aptamer with a low equilibrium dissociation constant was used as a biorecognition molecule.
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Here we investigated whether DNA nanostructures could be used to enhance the function of PD-L1 aptamers.
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