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Of these methods only immunohistochemistry measures protein expression, via classification of the level of staining, and the other methods quantify gene expression via measurement of mRNA copy number.
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The benefit of using CAI is that it can be computed for any gene with a codon frequency distribution, whereas experimentally measured protein expression or ribosomal loading data are often limited to relatively highly expressed proteins or transcripts.
Additionally, immunostaining was used to measure protein expression.
Such techniques are valuable to measure protein expression, solubility, activity, and native posttranslational modification events in heterologous systems.
However, the ability to measure protein expression, produce proteins (usually in recombinant form) and to block receptor ligand interactions remains essential for elucidating the function of the molecules of interest.
Immunohistochemistry was used to measure protein expression of MKP1 and CD31 and to assess cellular apoptosis.
It is majorly used to measure protein expression levels and the intensities of specific bands by using an online software tool (Gelquant.NET).
The term protein expression is however very rarely used in this sense, but tends rather to be used in the context of translation or protein synthesis, which is semantically not correct and further leads to misunderstandings when attempts are made to measure protein expression by two-dimensional gel electrophoresis or liquid chromatography.
Western blotting was used to measure protein expression levels of uPAR, COX2, and c-MET.
In these experiments, we measured protein expression levels of all the NADPH oxidase subunits.
As an indicator of Nrf2 activity in vivo, we measured protein expression of NQO1 in lung homogenates.
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