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. 2013 Jan 8;108(2):351–360. doi: 10.1038/bjc.2012.552

Figure 2.

Figure 2

Immunological validation of ubiquitin and S100P. (A) For ubiquitin, four BC and corresponding AT extracts were analysed by immunoblotting, indicating relative upregulation of ubiquitin in some breast cancer patients. β-Actin is shown as a loading control. (B) Densitometric analysis of ubiquitin western blots of eight sample pairs. Box plot shows median and upper and lower quartiles; lines show maximum and minimum values. P=0.017, Wilcoxon signed-rank test. (C) Mass spectrometry (MS) spectra of proteins bound to immobilised mouse anti-ubiquitin antibody. Samples were (i) patient 1 normal tissue, (ii) patient 1 cancer tissue, (iii) patient 2 normal tissue, (iv) patient 2 cancer tissue, (v) recombinant His-tagged ubiquitin, and (vi) patient 2 cancer tissue, mouse IgG control. Arrow indicates the mass of monomeric ubiquitin, m/z 8558. N=normal tissue; C=cancer tissue. (D) For S100P, four BC and corresponding AT extracts were analysed by immunoblotting, indicating relative upregulation of S100P in some breast cancer patients. β-Actin is shown as a loading control. (E) Densitometric analysis of S100P Western blots of 8 sample pairs. Box plot shows median and upper and lower quartiles; lines show maximum and minimum values. P=0.012, Wilcoxon signed-rank test. (F) Mass spectrometry spectra of proteins bound to immobilised rabbit anti-S100P antibody. Samples were (i) patient 3 normal tissue, (ii) patient 3 cancer tissue, (iii) patient 4 normal tissue, (iv) patient 4 cancer tissue, (v) recombinant His-tagged S100P, and (vi) patient 4 cancer tissue, rabbit IgG control. Arrow indicates the mass of the S100P form of m/z 9226. N=normal tissue; C=cancer tissue.