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The loss of the slr1649 gene product and the complete segregation of the mutation were shown by immunoblot experiments using polyclonal antibodies generated against Slr1649 (Fig. 3B).
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6× His-tagged BCAL2985 overproduction was assessed by SDS-PAGE analysis and immunoblot experiments using a monoclonal anti-polyhistidine peroxidase conjugate clone HIS-1 antibody (diluted 1 2000, SIGMA) as previously described (Sousa et al. 2013).
In immunoblot experiments using a p53 null lung cancer cell transfected with mutant p53 (173 mutation), low micromolar concentrations of CP-31398 were found to increase PAB1620 (wild-type antibody) positive cells by five-fold after treatment for 6 h [ 83].
Serum complement factor and activity levels, brain mRNA expression levels measured by real-time PCR, and normalized brain protein expression levels measured by immunoblot experiments were compared among different treatment arms by using ANOVA followed with Tukey adjustment for multiple pairwise comparisons.
This was confirmed with an associated decrease in the expression of α4β2 subtypes indicated by immunoblot experiments.
These results have been confirmed by immunoblotting experiments.
We then prepared cell lysates from ADR-treated U2OS cells and performed co-immunoprecipitation experiments using normal rabbit serum (NRS) or polyclonal anti-HDAC6 antibody followed by immunoblotting with the indicated antibodies.
Regarding to AP/α-CEA-λ phage, we were able to stain CEA protein directly in immunoblotting experiment by using this double displaying phage.
The cell extracts were analyzed by immunoblot assays using anti-NRLuc or anti-CRLuc antibodies.
The proteins were analyzed by immunoblot assays using the anti-NRLuc antibody (left panel) or anti-CRLuc antibody (right panel).
Lysates were analyzed by immunoblot (top) using the indicated antibodies.
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