The Nter and Cter domains were subjected to mobility shift assay where conformation change on binding Ca2+ was visualized on a SDS-PAGE gel.
Our data, however, show that CMWs are subject to the same mobility restrictions that necessitated their appointment in the first place.
The purity of these recombinant proteins was monitored by coomassie blue staining assay (Fig. 1B), and then subjected to electropheresis mobility shift assay (EMSA).
Next, to determine whether down regulation of MCP-1, IL-6 and TNF-α by parthenolide is mediated through the sustained inhibition of DNA-binding activities of NF-κB factors, nuclear extracts from cells treated with or without the inhibitor for 24 h were subjected to electrophoretic mobility shift assay (EMSA) (Fig 2B).
Nuclear extracts, prepared with NE-PER Nuclear and Cytoplasmic Extraction Reagents (Pierce), were subjected to electrophoretic mobility shift assay using the LightShift Chemiluminescent kit (Pierce).
Nuclear proteins were extracted from treated or untreated endothelial cells and subjected to electrophoretic mobility gel shift assay, as previously described [ 25].
Next, various segments of the 5′-upstream region of CYS3 were PCR-amplified (Fig. 3a) and subjected to electrophoretic mobility shift assays in the presence of extracts prepared from wild-type cells grown in SF medium (Fig. 3b).
The rationale for this has been postulated by Khan et al, 1 who pointed out that knee wounds are considerably longer than hip wounds and are subjected to more mobility as they are covered by less tissue.
Nuclear and cytoplasmic proteins were fractionated as previously described [ 21]. 15 μg of nuclear extracts (NE) were subjected to Electrophoretic Mobility Shift Assay (EMSA) using the high-affinity NF-κB-binding site [ 22].
The Monkey King element identified in the promoter of BnFLC.A10 in our previous study [ 31], was used to check the potential ability of Monkey King to regulate gene expression via DNA methylation and was subjected to electrophoretic mobility shift assay (EMSA) analysis to check for interacting proteins.
