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Protein extracts from non-transduced cultures were also submitted to western blot in order to discard changes in LC3-II level after lentiviral transduction; no differences were observed.
Some immunoblot images of a given target were cropped from the same blot in order to conserve figure space and redundancy.
p53 protein levels were assessed by Western blot in order to confirm accumulation of this tumour suppressor in response to the BaP concentrations used in this study.
The samples were compared in terms of expression of metabolic, EMT, TIC and CAF markers, and analysed by western blot in order to specifically assess the net outcome of genetic, epigenetic and post-translational effects.
These enzymes were additionally tested to assure that there was no cutting site within the 16S region, where the detection probe hybridizes during the Southern Blot, in order to prevent occurrence of too many bands resulting from binding of the probe to cut target sequences.
Bovine primary fibroblasts were infected with either SBV, SBVdelNSs or mock-infected and RNA was extracted at 16 h p.i.. Three biological replicates were assesses for each sample and cells were also infected in parallel for immunofluorescence and Western blot in order to confirm that the bovine primary cells were infected by SBV and SBVdelNSs at 16 h.
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We circumvented this complication by performing 2D gel electrophoresis combined with Western blotting in order to monitor possible changes to the isoelectric points of transport components.
To ascertain that the PTS phosphorylation cascade is also functional in vivo we used Western blots in order to demonstrate the presence of P∼EIIANtr in B. melitensis crude extracts.
We performed Western blots in order to: (i) Confirm that FOXO1a protein expression level is elevated in human compared to chimpanzees, and (ii) confirm the FOXO1a knockdown in HepG2/C3A liver cells (see below).
We used Northern blotting in order to test whether p73β controls Noxa expression in p65 null cells.
Band densities of acetylation specific blots were normalized to the respective densities of total histone H3 blots in order to obtain specific acetylation rates for each sample.
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