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After washing, the bound proteins were analyzed by western blotting using an anti-Rac1 antibody.
After resuspending with AS buffer, the membranes and their bound proteins were analyzed by SDS-PAGE and Western blotting.
The bound proteins were analyzed by immunoblotting with the indicated antibodies.
Bound proteins were analyzed by Western blot with anti-CD4 antibody (Fig. 4A).
Bound proteins were analyzed by Western blotting with anti-GFP (Fig. 2D).
After 4 days of differentiation, cell extracts were prepared without detergent, incubated with 7-methyl-GTP (m7-GTP) Sepharose beads, and the bound proteins were analyzed by immunoblot.
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Each fraction eluted from the affinity gel, using elution buffer containing HA peptide (Roche Applied Science) as binding competitor to displace the bound proteins, was analyzed by SDS-PAGE, and scFvG2/p17 or scFvE2/p17 detected by Western blotting, using anti-HA tag antibody, as described below.
The bead-bound proteins were analyzed as previously described [5].
Glutathione-Sepharose-bound proteins were analyzed by Western blotting with specific monoclonal antibodies (mAbs) against p120-catenin, β-catenin, E-cadherin, N-cadherin (all from BD Biosciences).
After 120 min, chromatin-bound proteins were analyzed by immunoblotting.
Then, the SETD6-bound proteins were analyzed and identified by mass spectrometry as described elsewhere.
More suggestions(18)
induced proteins were analyzed
related proteins were analyzed
bound proteins were analysed
bound proteins were removed
bound proteins were eluted
bound fractions were analyzed
bound proteins were solubilized
bound proteins were detected
bound proteins were separated
bound fragments were analyzed
bound proteins were visualized
bound regions were analyzed
bound proteins were released
bound proteins were subjected
bound proteins were recovered
bound complexes were analyzed
bound proteins was analyzed
bound proteins were washed
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