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By means of gene fragmentation, six overlapping peptides were expressed in Escherichia coli, and their IgE binding activity was evaluated by immunoblotting in a cohort of 79 Parietaria-allergic patients.
Nuclear extracts were prepared and phosphorylated and dephosphorylated c-Jun isoforms were detected by Western blot analysis and the DNA binding activity was evaluated by electrophoretic mobility shift assay.
Crf2 binding activity was evaluated by antigen ELISA (Fig. 9, Table 3).
The NF-κB binding activity was evaluated using a LightShift Chemiluminescent EMSA kit (Pierce, Rockford, IL, USA).
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Several isobenzofuranone derivatives were synthesized and their PKCα binding activities were evaluated.
NF-κB activity was evaluated by binding of 60 µg of tissue extracts of tissue or 8 10 µg of nuclear extracts from cells, as described [18].
Their antiviral activity was evaluated and molecular modeling was utilized to give further envision on their probable binding modes in the allosteric binding site.
AChE activity was evaluated according to [20].
Anticancer activity was evaluated.
In addition, the ALDH activity was evaluated.
The in vitro binding affinity on anti-apoptotic Bcl-2 proteins and cell killing activity were evaluated.
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