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For the protein profile of FBS and HS depicted in Fig. 12 and the Western blot experiments shown in Fig. 18, the concentration of proteins loaded onto each lane was evaluated using the Bradford colorimetric protein assay (Biorad, Hercules, CA, USA).
For Western blot experiments shown in Figure 4, embryos were dechorionated and taken up in ice-cold PBS buffer containing 0.01% Triton.
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For the whole cell extraction and Western blotting experiments shown in Figure 8, AC16 cells were seeded at ~1 × 10 cells per 10 cm diameter plate and treated as described above.
Our Western blot experiments showed that in the presence of DMPO, the Cu,Zn-SOD–(bi sulfite system produced sulfite-derived radicals that oxidized albumin to produce protein-centered radicals trapped by the nitrone spin-trap DMPO and detected as DMPO-HSA nitrone adducts.
This was confirmed by SDS PAGE and Western blot experiments showing similar β-tubulin levels in COS1 cells transfected with the different parkin variants (not shown), thus assuring similar amounts of cellular input material.
The latter conclusion was directly supported by Western blot experiments showing activation of caspase-8 in NB cells following CD40 CD40L interaction and its block by exposure to the Z-LE-TD-FMK inhibitor.
However, western blot experiments showed that p53 monomers are also present in trophoblast.
Western blot experiments showed that the protein level of AdipoR1 in the striatum, cortex, and hippocampus was reduced in the HFD group.
In facts, western blot experiments showed that, Vitronectin interacts with our NPs system, while experiments with echistatin, clearly underlined the role of avb3 integrin in the NPs modulation of cell viability and uptake.
Western blot experiments showed that also the uPAR protein was increased in tumor tissues by 1.83 ± 0.15 fold (p < 0.01).
Western blot experiments showed that IR phosphorylation was reduced by Mut in a concentration dependent manner suggesting a dominant negative effect.
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