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To demonstrate that the expression of recombinant peptide originally examined using a gag sequence was not insert specific or unique, this study examined recombinant SD109 transformants expression of the three different SIV encoded peptides within the framework of recombinant GvpC protein.
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As with our results, the combined overexpression of ctfA, ctfB and adc increased the solvent production by transformants, whereas expression of adc gene alone had little effect.
Indeed, wild-type and s* nuclei could be recovered through the isolation of microconidia in such transformants, before expression of a Secteur, indicating that the S → s* thalli had a heterokaryotic structure.
Only one of seven potential TDR transformants (transformant 5) showed expression of both genes (Fig. 2b), which was used for further analysis for alkane production.
In addition, two of fifteen transformants showed additional expression of the reporter gene in the anthers when assayed under standard conditions, and fourteen out of fifteen transformants showed this staining when assayed at a higher substrate concentrations.
Stable transformants showed the expression of GFP as detected by confocal microscopy.
Interaction of the two fusion proteins in co-transformants drives the expression of the yeast His3 gene, which is required for growth of the histidine-auxotrophic E. coli host on selective plates (see Materials and methods for details).
This may be due to a random insertion of the recombinant plasmid that may have affected the sporulation pathway of the transformants and modified the expression of sporulation-related genes (Park et al. 2013; Yu et al. 2015).
Stable transformants were selected for expression of hDHFR.
In particular, NsbHLH2 expression of transformants decreased dramatically under the osmotic stress, based on our qRT-PCR results (Fig. 2a).
Nevertheless, transformants showed significantly increased expression of total NsbHLH2 RNA, and we observed increased growth rate and biomass productivity under osmotic stress.
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