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All spectral data were normalized by total ion current after background subtraction. The mass range of peaks was analyzed between 1.5 and 30 kDa, because the majority of resolved protein/peptides were found in this range. Molecular http://en.wikipedia.org/wiki/MERTK masses from 0 to 1.5 kDa were mainly the signal noises of the EAM and were excluded from this analysis. The Biomarker Wizard (Ciphergen Biosystems) was subsequently used to make peak detection and cluster across all spectra with the following settings: signal/noise (first pass): 5; minimum peak threshold: 10% of all; mass error: 0.3%; and signal/noise (second pass): 2 for the 1.5 to 30 kDa mass range to avoid the miscounting of the protein peaks. The statistical significance of the peak height difference between samples from the two groups was calculated using the 2-sample t-test. Serum levels of eight protein peaks with molecular weights ranging from 1.5 to 30 kDa were statistically different in 24 preoperative and 23 postoperative (without relapse) breast cancer samples (P http://www.selleckchem.com/products/SRT1720.html statistically different expression between preoperative patients and postoperative patients without relapse (P = 0.000004). Moreover, a statistical difference of 3964 m/z was also observed between the postoperative group (without cancer relapse) and postoperative group (with cancer relapse), P = 0.0085. Detailed protein spectra data for the three groups is presented in Fig. 1. Cancer is a multifactorial disease, which develops as a multiple-stage process involving the accumulation of genetic, http://www.selleckchem.com/products/Adrucil(Fluorouracil).html epigenetic, and eventually proteomic changes. Proteins and peptides from cancer cells are secreted into the blood, which may allow an opportunity for the blood-based detection of disease-specific proteomic changes. Proteomics provides us with a dynamic picture of protein levels and protein modifications (Brozkova et al., 2008), which could reflect disease stages and development. Disease biomarker discovery used to be a laborious enterprise. SELDI-TOF MS combines retention with MS in which proteins are captured by adsorption, partition, electrostatic interaction, or affinity chromatography on a solid-phase protein chip surface. This technology thus provides a unique sample preparation platform and facilitates the discovery of protein markers (Garrisi et al., 2008; Gon?alves et al., 2008; Gast et al., 2009a; Zeidan et al., 2009).