According to the manufacturer's instructions, protein extracts were prepared and incubated with the nitrocellulose membranes, followed by detection of specific protein binding with biotinylated secondary antibodies using streptavidin-HRP and chemiluminescence detection reagents.
According to the manufacturer's instructions, protein extracts were prepared, incubated with the nitrocellulose membranes, followed by detection of specific protein binding with biotinylated secondary antibodies using streptavidin-HRP and chemiluminescence detection reagents.
Two rounds of biotinylated bait-based hybridizations were performed, followed by binding with streptavidin magnetic beads, a washing step, and an elution step.
With this method, amplification and detection are achieved by covalently coupling photoinitiator molecules to streptavidin proteins followed by binding onto biotinylated oligonucleotide targets immobilized to a biosensor surface.
This hypothesis was further confirmed by binding studies using biotinylated cyclotraxin-B.
Specificity was determined using non-specific oligomer as well by competing the binding with non-biotinylated oligomer supplied in the kit.
We determined non-specific binding by performing incubations with biotinylated 15d-PGJ2 in the presence of 100 µM unlabeled 15d-PGJ2.
After extensive washing, binding of TNFα was detected by incubation with biotinylated antibodies, followed by streptavidin-peroxidase; colorimetric enzyme assays were performed to detect bound TNFα.
After washing in PBS, the sites of primary antibody binding were localised by sequential incubation with biotinylated goat anti-rabbit antibody and then streptavidin conjugated with horseradish peroxidase.
Primary antibodies were incubated overnight, followed by labeling with biotinylated secondary antibodies and horseradish peroxidase-conjugated neutravidin.
