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Proteomics was developed in the early 1990s to allow proteins expressed by cells and tissues to be systematically studied (Celis et al., 1999; Arrell et al., 2001). The word proteome was coined by Marc Wilkins et al (Wilkins et al, 1996) from the words “protein and genome”. It is therefore defined as protein equivalent of the genome. Generally, unique spectrum of proteins is only synthesized by specific cell types, for example amylase is secreted by the parotid gland, insulin by the pancreas and thyroxin by thyroid follicles. Protein synthesis is a complicated process formed by the different combination and length of the 20 unique amino acids found in our body (Arnstein, 1965). For example, following the transcription of genes encoded in the DNA, the mRNAs translocate into the cytoplasm where they are translated into a specific type of protein by the ribosomes (Lengyel, 1966). This is then followed by post-translational modification of the peptide chain to configure the protein so that it becomes biologically active. Post-translational modifications of proteins involve glycosylation, alkylation, methylation and sulfation (Blundell et al., 1993, Fleischer, 1983). The coand post-translational modifications allow the protein to be transported and secreted during cellular homeostasis (Finnerty et al., 1979; Mao et al., 2011). In this chapter, we have described the comparative 2-dimensional electrophoresis (2-DE) proteomics workflow for protein identification by mass spectometry. Comparative proteomics was used

Comparative Proteomics: An Approach to Elucidating the Function of a Novel Gene Called BRE