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G-CSF induced strong binding to this probe, which was also blocked by both JAK2 and STAT3 inhibitors.
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Evidently, addition of a 250-fold excess unlabelled fragment completely outcompeted the binding to the probe, indicating that this ICS1 promoter fragment specifically interacted with WRKY28.
Then, binding to these probes by purified recombinant AtClpC2 and AtClpD was analyzed.
This corresponds to greater binding to NFκB probe as revealed by mobility shift assays (Fig. 5B).
(C ) M ybx1 sa42 embryo extracts show no detectable binding to sqt1 probe compared to control extracts.
However, it was not possible to see in vitro Zur binding to the DNA probe containing this promoter.
The binding to the −151T probe was competed with 200-fold molar excess of unlabeled probe.
Since excess unlabeled NF-κB oligonucleotide competed out DNA binding to the κB probe, NF-κB binding was considered specific.
The binding of this probe to the cell membrane depends on the surface potential, which modulates the binding constant to the membrane.
We denote by F i) the (unobserved) binding probability of the TF to this probe.
Evaluation by FP showed binding of this probe to JHDM1A.
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