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Antigen binding ELISAs were also carried out to determine the relative amount of biochemically active recombinant protein in each preparation.
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In addition, DNA binding activity of nuclear NF-κB p65, as demonstrated by highly sensitive and specific ELISA, was also inhibited in OA chondrocytes.
A competitive ELISA was also performed to study the ability of GM-1111 to inhibit/compete RAGE binding to its ligands.
Enzyme-linked immunosorbent assay (ELISA) was also employed to confirm the biological specificity of these surfaces.
ELISA was also used to confirm successful VEGF attachment.
Several peptides with mutation within the PDZ binding motif were also included in the ELISA-based affinity study.
Plasma concentrations of the monovalent anti-IL-6R binding domain were also measured using a sandwich ELISA.
TNFα ELISA results were also confirmed by this assay.
Each conjugate bound HER2 with affinity similar to that of trastuzumab, and comparable binding was also seen by ELISA (SI Figure S3).
They were also tested in ELISA to validate their binding to CLDN1 exposed on the surface of HEK-293 cells.
Plasma samples were also analysed for binding to CEA coated ELISA plates as a measure of immunoreactivity.
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