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Western blotting analyses using the anti-nNOS antibody revealed the presence of one band at 155 KDa.
Total RNA was isolated from the two youngest expanded leaves or shoot apices and subjected to real-time RT-PCR or Northern (RNA) blotting analyses using the constitutively expressed EF1α and/or Actin2 genes as references.
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The resolved proteins were transferred to nitrocellulose membranes and detected by Western blotting analyses using antibodies as indicated.
We therefore carried out Western blotting analyses using antibodies made against phosphorylated tyrosine (p-tyr) on cell subjected to calcium uncaging.
Their transgenic status was confirmed by genomic PCR and western blotting analyses using anti-AtPAP2 antibodies.
We carried out northern blot analyses using the sequences of OsPDS and OsSLR1 Gene Specific Tags (GST) as probes to hybridize sequentially the same membranes.
The purity of the protein was determined by SDS-PAGE with Coomassie Blue staining and Western blot analyses using the anti-truncated SDH domain of LKR/SDH mouse sera.
To elucidate the expressions of F3H, F3′H, and F3′5′H, we next performed northern blot analyses using the same RNAs.
We then performed Western blot analyses using the same developmental stage samples used for SDS-PAGE and blotting as described above.
Western blot analyses using the anti-IFT27 antibody showed a single band migrating at a position close to the predicted size of 20 kDa in wild-type cells.
To obtain proof that H3.7 is targeted by the specific acetylation that was detected using the H3K36ac antibody (GVKacKPHR), we performed Western blot analyses using the same samples as described above, in combination with PTM-specific antibodies.
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