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No binding was detected to GST alone (Fig. 3A, lane 2).
No binding was detected to either tunicamycin-treated or untreated AGM cells (Figure 4B).
Consistent with our flow cytometric analysis, laminin binding was detected to α-DG from DN2 through DN4 stages but not to DP and single positive thymocytes (Fig. 1B, top).
No binding was detected to GST, therefore demonstrating a direct interaction to HESX1 and confirming previous results using in vitro translated DNMT1.
As shown in Figure 6A D, soluble trimer in SAS elicited responses against the V3 peptide and these sera bound the V1 epitope at the highest (5 μg) immunization dose, but no binding was detected to V2 or the MPER sequence.
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Similarly, binding of MITF was detected to predicted E-box sites upstream of six of the genes induced by inhibition of PI 3-kinase.
Strong binding of KSHV1 51 EGFP) and RFHV1 50 EGFP) was detected to importins α1, α3, α5, α7 (Fig. 5, lanes 3,4,5 and 6) with α3 showing the most robust binding.
DNA binding was detected according to LightShift chemiluminescent EMSA kit (Pierce, Rockford, IL) (Han et al, 2006).
However, strong binding of ksI+II20 49 EGFP) and rfI+II20 48 EGFP) was detected to both importin α3 and importin β1Δ (Fig. 3A,B, lanes 9 and 10, respectively).
Upon the addition of OMAB to the immobilized Aβ fibrils, a strong, but highly substoichiometric binding was detected, which corresponded to a molar ratio of about 1∶2000 OMAB Aβ.
The R&D anti-CXCR3 antibody was not directly conjugated to any fluorophore, so cell binding was detected with a secondary antibody conjugated to PE.
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