The world of global proteome profiling is rapidly expanding, spurred by advances in stable isotope labeling techniques. While many stable isotope incorportation methods are available, the most proven, simplest, efficient method remains the well-characterized trypsin-mediated incorporation of 18O.
As early as 1993, 18O stable isotope labeling measured by mass spectrometry was used to measure differential expression of proteins of interest. Since then, it has proven a successful tool to study proteomic differences in human and mouse plasma, secretory proteins from rat adipose cells, the detergent-resistant membrane proteome, proteome profiles of ductal carcinoma cells and the drug susceptible MCF-7 human breast cancer cell line, and many other significant scientific inquiries as well.
Convenient, efficient, and affordable, the ProteomeProfiler 18O Enzymatic Labeling Kit provides the reagents, techware, and an optimized method required to perform this time-tested strategy. Well characterized and trusted, 18O labeling is the proven solution for your global proteome profiling needs.
Efficient Trypsin Mediated 18O Incorporation
Discover improved expression profiling with the enzymatic incorporation of a stable 18O isotope label. In the presence of a protease such as trypsin, oxygen atoms from H18OH will specifically exchange with the two oxygen atoms of the carboxyl terminus of each tryptic peptide. The incorporation of two 18O atoms results in a 4 Da mass shift, which is readily observed when analyzed by mass spectrometry. The mass shift allows labeled and unlabeled samples to be pooled and analyzed for differential expression.