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Recent advances in bottom-up proteomics using targeted LC-MS have enabled previously unachievable identification and quantification of target proteins and posttranslational modifications within complex samples.
The development of quantitative proteomics has enabled the absolute quantification of target proteins (i.e., target proteomics).
Use of internal reference gene(s) is necessary for adequate quantification of target gene expression by RT-PCR.
In this study, a new method for the absolute quantification of target proteins was developed by combining dimethyl labeling with SID-MRM mass spectrometry.
The absolute quantification of target proteins in proteomics involves stable isotope dilution coupled with multiple reactions monitoring mass spectrometry (SID-MRM-MS).
Three replicates were performed for each reaction, and OsActin1 was used as an internal control for the relative quantification of target gene expression.
Furthermore, chemical ionization quadrupole mass spectrometer which is available switching between EI and CI techniques was suited better than EI-fast TOFMS for the quantification of target alkylpyrazines.
In addition, it was capable of accurate quantification of target RNA molecules independently of the presence of DNA in the sample.
Sensitive, reliable and reproducible quantification of target rDNA could be achieved applying primer — probe combinations that mediate in vitro amplification of DNA fragments smaller than 100 base pairs.
Relative quantification of target DNA present in unknown samples was performed by comparison of the fluorescence signals of the samples to those obtained from plasmid standard dilutions.
The designed immunosensor was amenable to direct quantification of target protein with a wide range of concentration in complex clinical serum specimens.
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