Mass spectra were generated on an automated System 4000 Bio-Rad ProteinChipH reader. Mass spectra data were collected and analysed using the ProteinChipH Data Manager Client 3.5 software (BioRad Inc.). Spectra were generated at both high (3,000 nJ) and low (1,600 nJ) laser energies with mass focus set to 40,000 Da and 6,000 Da respectively. Spectra were normalised by total ion current starting with a minimum mass/charge (m/z) of 2,500. Spectra with normalisation factor outside mean 62 standard deviations were removed. The remaining spectra were re-normalised by total ion current. Spectral peaks corresponding to mass/charge (m/z) clusters were detected and clustered using the ProteinChipH Data Manager Client 3.5 software (BioRad Inc.) by auto-detecting peaks to clusters in two steps. For the first step a signal to noise ratio of 5 and valley depth of 3 were used, with a minimum peak threshold of 20% of all spectra. For the second step a signal to noise ratio of 3 and valley depth of 1 were chosen. The cluster window was set at 1.0 peak width and expression difference mapping performed over m/z range of 2,500 to 200,000. Instrument calibration was performed using All-in-1 Peptide and Protein calibrants (Bio-Rad). Reproducibility was determined by measuring the inter-ProteinChipH coefficient of variation (CV) for the quality control spectra, based on all peaks in the spectrum with intensity .1 mA. Overall interchip CV for the quality control sample was 20%, consistent with similar studies.