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Ponceau staining of membranes was used to monitor protein transfer and loading.
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Another is time-resolved luminescence resonance energy transfer (LRET), which has been used to monitor protein interactions in cells; this technique takes advantage of a luminescent terbium complex and luminescent energy transfer to GFP [ 30].
Especially fluorescence resonance energy transfer (FRET) between suitable GFPs has received widespread attention as it allows, in principle, to monitor protein conformations and protein-protein interactions inside living cells [ 2].
Cell-free extracts (60 µg protein) were loaded on 12% 1-D SDS PAGE (Invitrogen) and resolved proteins from several mini-gels were transferred to the same PVDF membrane (Millipore) so that one set of samples was used to monitor protein loading using β-Actin.
Protein transfer was confirmed by Ponceau staining.
Protein transfer was checked by Ponceau staining.
Protein transfer was evaluated by Ponceau staining.
HSC70 was used to monitor protein loading.
Such proteins include sphingolipid activator proteins, CD1 proteins, ceramide transfer protein, phosphoglyceride transfer proteins, other START-related proteins, nonspecific lipid transfer proteins, fatty acid binding proteins, lipocalins, and plant lipid transfer proteins [ 13, 16, 17].
Commonly employed approaches for monitoring protein kinase activity include quantitative radioactivity-based approaches that rely on phosphoryl transfer from [γ-32/33P]ATP [γ-32/33P]ATP protoin substrates, semiquantitative peptideprorein-sprotein antibody-basubstratessemiquantitativetrometry-based phosphoproteomics analyses.
Ponceau S staining was used to monitor uniform transfer of protein.
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