| Autor: |
Bowser BL; Department of Chemistry, Vanderbilt University, Nashville, Tennessee, USA; email: rena.as.robinson@vanderbilt.edu., Robinson RAS; Department of Chemistry, Vanderbilt University, Nashville, Tennessee, USA; email: rena.as.robinson@vanderbilt.edu.; Department of Neurology, Vanderbilt University Medical Center, Vanderbilt University, Nashville, Tennessee, USA.; Vanderbilt Memory and Alzheimer's Center, Nashville, Tennessee, USA.; Vanderbilt Institute of Chemical Biology, Vanderbilt School of Medicine, Nashville, Tennessee, USA.; Vanderbilt Brain Institute, Vanderbilt School of Medicine, Nashville, Tennessee, USA. |
| Abstrakt: |
The identification of thousands of proteins and their relative levels of expression has furthered understanding of biological processes and disease and stimulated new systems biology hypotheses. Quantitative proteomics workflows that rely on analytical assays such as mass spectrometry have facilitated high-throughput measurements of proteins partially due to multiplexing. Multiplexing allows proteome differences across multiple samples to be measured simultaneously, resulting in more accurate quantitation, increased statistical robustness, reduced analysis times, and lower experimental costs. The number of samples that can be multiplexed has evolved from as few as two to more than 50, with studies involving more than 10 samples being denoted as enhanced multiplexing or hyperplexing. In this review, we give an update on emerging multiplexing proteomics techniques and highlight advantages and limitations for enhanced multiplexing strategies. |
